CN1531587A

CN1531587A - Detergent compositions comprising cyclodextrin glucanotrasferase enzyme

Info

Publication number: CN1531587A
Application number: CNA008198586A
Authority: CN
Inventors: J��÷��͢��; J·斯梅茨; A·平滕斯
Original assignee: Procter and Gamble Ltd
Current assignee: Procter and Gamble Ltd
Priority date: 2000-06-30
Filing date: 2000-06-30
Publication date: 2004-09-22
Also published as: AU2000260630A1; EP1294844A1; HUP0300967A2; CA2412371A1; MXPA03000119A; BR0017277A; JP2004502831A; WO2002002725A1; CZ20024166A3

Abstract

The present invention relates to detergent compositions, including laundry, dishwashing, and/or hard surface cleaner compositions, comprising a cyclodextrin glucanotransferase enzyme and a detergent ingredient selected from a nonionic surfactant, a protease and/or a bleaching agent. Such compositions provide excellent removal of starch-containing stains and soils and malodor control; and when formulated as laundry compositions, excellent whiteness maintenance and dingy cleaning.

Description

Detergent compositions comprising cyclodextrin glucanotransferase

Technical Field

The present invention relates to detergent compositions comprising a cyclodextrin transferase and a detergent ingredient selected from a nonionic surfactant, a protease and/or a bleach.

Background

The performance of a detergent product is determined by a number of factors, including the ability to remove soils. Thus, detergent components such as surfactants, bleaches and enzymes have been incorporated into detergents, one of such specific examples being the use of proteases, lipases, amylases and/or cellulases.

In particular, it has long been recognized that amylases in detergent compositions can remove starchy food residues or starch films from dishware or hard surfaces or provide cleaning performance on starchy soils as well as other soils typically encountered in laundry and dishwashing applications. Indeed, starchy materials, such as amylose and amylopectin, are a major component of the soils/stains encountered in laundry, dishwashing or hard surface cleaning operations. In addition, the textile industry also uses starch-based materials in their textile finishing processes. Thus, amylases have long been incorporated into detergent products to remove starch-containing stains. However, we have surprisingly found that such commonly used detergent amylases are not capable of hydrolysing retrograded starch or raw starch.

Radley is a term used to describe changes in Starch pastes that occur spontaneously or upon aging as studied in J.A. Radley, Starch and its Derivatives, fourth edition, Chapman and Hall Ltd, page 194-201. This is due to the inherent tendency of starch molecules to bind to each other and can result in increased crystallinity. Solutions of low concentration become increasingly cloudy as starch molecules gradually associate into larger particles. Spontaneous precipitation occurs and the precipitated starch appears to revert to its original state of being cold water insoluble. Higher concentrations of paste gel upon cooling, which gel becomes increasingly harder upon aging due to increased association of starch molecules. This is due to the strong tendency of hydrogen bonds to form between the hydroxyl groups on adjacent starch molecules.

The changes that occur during retrograding are of considerable importance in the industrial application of starch, which is considered to be an important factor in the aging of bread and the structural changes of other starchy foods, such as canned soups, beans, meat products, etc. Starch and retrograded starch have also found use in the textile, paper and adhesive industries. In practice, fabrics are sized with starch in fabric processing. Depending on the sizing process, retrograded starch may form on the fabric and it cannot be removed in a subsequent desizing process. Furthermore, most stains/soils present on fabrics, dishware and other hard surfaces, especially those found in the kitchen, contain starch which, upon ageing, for example, will reverse such an associated starch network in a laundry basket or dish washer. Such retrograded starchy materials are therefore subsequently found on the fabrics, dishes and/or hard surfaces to be cleaned. This retrograded starch shows an increased resistance to hydrolysis by amylolytic enzymes, is only slightly soluble at normal temperature and is also difficult to redisperse, especially if the retrograded starch has been previously dried, and it furthermore shows an increasing gel firmness. In fact, retrograded starch has been found to form very stable structures and to melt only at very high temperatures, such as 150 ℃ for amylose, 60 ℃ for amylopectin or 120 ℃ for complex amylose lipids. The degree and time of retrogradation depends on the starch type, which can vary between 10% and 90% starch content. It has now been found that current detergent amylases have hardly any effect on retrograded starch.

In addition, a substantial portion of the starchy material remains in a substantially raw state, even when processed in the food or textile industry. In particular, it has been found that food stains such as rice, spaghetti, potatoes, corn, cereals and the like recovered on fabrics, tableware and other hard surfaces contain substantial amounts of raw starch.

Furthermore, it has been surprisingly found that such retrograded or raw starch, which remains on the surface, also further entraps dirt and, when present on the fabric surface, results in a dirty appearance of the surface to be cleaned.

From the foregoing, it can be seen that there is a need to formulate detergent products which are capable of removing such raw or retrograde starchy soils/stains. Thus, the above objects have been achieved by formulating detergent compositions comprising a maltogenic alpha-amylase enzyme and a detergent ingredient selected from the group consisting of nonionic surfactants, proteases and/or bleaches.

Indeed, it has been surprisingly found that the combination of a nonionic surfactant and a cyclodextrin glucanotransferase enzyme in a detergent composition provides a very effective ability to remove starch-containing stains and soils. In fact, it has been found that cyclodextrin glucanotransferase has transferase activity on starch as well as endo and exo hydrolytic activity, which is very useful for cleaning applications. In addition, such starch-containing stains and soils also include a number of lipid components. Without wishing to be bound by theory, it is believed that the nonionic surfactant removes lipids contained in the starch-containing stains and soils, thereby promoting degradation of the starch by cyclodextrin glucanotransferase. In addition, it is believed that the nonionic surfactant will keep the degraded starch in solution and prevent it from redepositing onto the surface to be cleaned. We have also surprisingly found that nonionic surfactants prevent retrogradation of starch and are therefore very effective if used in a pre-treatment step with cyclodextrin glucanotransferase. Similarly, such starch-containing stains and soils also include a number of protein components. Without wishing to be bound by theory, it is believed that the protease is capable of hydrolyzing the proteins contained in such complex stains and thereby rendering such stains/soils synergistically removable with the cyclodextrin glucanotransferase enzyme. In addition, such hydrolyzed protein/starch-containing stains/soils have a relatively low molecular weight in the wash solution, which may render such hydrolyzed stains/soils insufficient for redeposition onto the surface to be cleaned. Finally, it has been found that bleaching agents oxidize starch-containing stains and soils. Without wishing to be bound by theory, it is believed that the oxidation of the bleaching agent results in starch being more soluble and therefore more synergistically removed by the cyclodextrin glucanotransferase enzyme and the bleaching agent, while it also results in insufficient soil redeposition onto the surface being cleaned.

Furthermore, it has been surprisingly found that the combination of a nonionic surfactant and/or protease and cyclodextrin glucanotransferase provides synergistic malodor control. It is believed that the main source of malodour originates from e.g. greasy substances trapped in complex dirt/stains. Without wishing to be bound by theory, it is believed that the nonionic surfactant removes lipids contained in starch-containing stains and soils. Similarly, binding to a protease will enhance starch removal. This promotes the degradation of starch by means of cyclodextrin glucanotransferase. Thus, due to the enzymatic activity of cyclodextrin glucanotransferase, more starch is available to form cyclodextrin. Cyclodextrins are known to contain hydrophobic cavities which can entrap hydrophobic molecules and thereby remove malodorous substances. The combined action of the nonionic surfactant and/or protease and cyclodextrin glucanotransferase results in the production of more cyclodextrin and the removal of more entrapped malodorous substances, thus resulting in better malodor control. Furthermore, it has been found that the oxidising action of the bleaching agent has a sanitising effect in preventing the growth of microorganisms and the malodour formed thereby on the surface to be cleaned.

Cyclodextrin glucanotransferases find application in processes for the manufacture of cyclodextrins for a variety of industrial applications, particularly in the food, cosmetic, chemical, agrochemical and pharmaceutical industries. Cyclodextrin glucanotransferases may also be used in processes for the manufacture of linear oligosaccharides, especially linear oligosaccharides having 2 to 12 glucose units. Cyclodextrin glucanotransferases are also used in the in situ generation of cyclodextrins, particularly in processes for the production of baked products, in processes for the stabilization of chemical products during their manufacture, and in detergent compositions. Certain cyclodextrins are known to improve the quality of baked products. Cyclodextrins have inclusion capacity and can be used for stabilization, solubilization, and the like. Cyclodextrins thus stabilize oxidizing and photolytic substances, make volatile substances nonvolatile, make poorly soluble substances soluble and make odoriferous substances odorless, etc., and thus can be used to encapsulate perfumes, vitamins, dyes, drugs, insecticides and fungicides. Cyclodextrins can also bind lipophilic substances, such as cholesterol, to remove them from egg yolk, cream, etc. Cyclodextrins have also been used in products and processes related to plastics and rubber, where they have been used for different purposes in plastic laminates, films, membranes, and the like. Furthermore, cyclodextrins have been used to make biodegradable plastics. EP 802259 describes cyclodextrin transferases for the production of gamma-cyclodextrin. GB 169902 discloses polypeptides having cyclomaltodextrin glucanotransferase activity. JP07109488 describes detergent compositions comprising cyclodextrin transferase which have a high degree of detergency and deodorising action on starch. JP07107971 describes a specific cyclodextrin glucanotransferase enzyme from bacillus, which has an improved stability towards alkalines. WO96/33267 and WO99/15633 relate to specific novel variants of cyclomaltodextrin glucanotransferase.

However, the use of cyclodextrin transferases in conjunction with the synergy of detergent ingredients, particularly selected from nonionic surfactants, proteases and/or bleaches, in detergent compositions for the synergistic removal of starch-containing stain-soil and malodor control has not been recognized in the past.

Summary of The Invention

The present invention relates to detergent compositions, including laundry, dishwashing and/or hard surface cleaner compositions, comprising a cyclodextrin glucanotransferase enzyme and a detergent ingredient selected from a nonionic surfactant, a protease and/or a bleach. Such compositions provide excellent starch-containing stain and soil and malodor control, and when formulated into laundry compositions, excellent whiteness maintenance and dingy cleaning.

Detailed Description

Cyclodextrin glucanotransferase

The first essential component of the present invention is a cyclomaltodextrin glucanotransferase (e.c.2.4.1.19), also known as cyclodextrin glucanotransferase or cyclodextrin glycosyltransferase, hereinafter referred to as cgtase, which catalyzes the conversion of starch and similar substrates to cyclomaltodextrin through intramolecular transglycosylation reactions, thereby forming cyclomaltodextrins of various sizes, hereinafter referred to as cyclodextrins (or CDs). Commercially most important are cyclodextrins with 6,7 and 8 glucose units, which are referred to as a-, b-and g-cyclodextrins, respectively. Commercially of secondary importance are cyclodextrins with 9, 10 and 11 glucose units, which are referred to as d-, e-and z-cyclodextrins, respectively.

Cyclodextrins are cyclic glucose oligomers with hydrophobic internal cavities. They are capable of forming inclusion complexes with many small hydrophobic molecules in aqueous solutions, resulting in changes in physical properties, such as increased solubility and stability and decreased chemical reactivity and volatility. Cyclodextrins find application in particular in the food, cosmetic, chemical and pharmaceutical industries.

Most CGT-enzymes have both starch degrading and transglycosylation activities. Although some CGTases produce primarily a-cyclodextrin and some CGTases produce primarily b-cyclodextrin, CGTases typically form a mixture of a-, b-, and g-cyclodextrins. A selective precipitation step with an organic solvent can be used for the isolation of a-, b-and g-cyclodextrins. To avoid expensive and environmentally harmful steps, it is desirable to utilize cgtase enzymes that are capable of producing increased proportions of one particular type of cyclodextrin.

CGTzymes derived from different bacterial sources have been described in the literature, including CGTzymes obtained from Bacillus, Brevibacterium, Clostridium, Corynebacterium, Klebsiella, Micrococcus, Thermoanaerobacterium (Thermoanaerobacterium), and Thermoanaerobacterium (Thermoanaerobacterium).

Such as Kimura et al [ KimuraK, Kataoka S, Ishii Y, Takano T and YamaneK;J.Bacteriol.1987 169 4399-4402]bacillus species 1011 CGT enzymes, Kaneko et al [ Kaneko T, Hamamoto T and Horikoshi K;J.Gen. Microbiol.1988 134 97-105]bacillus species strains 38-2 CGT enzyme, Kaneko et al [ Kaneko T, Song KB, Hamamoto T, Kudo T and HorikoshiK;J.Gen.Microbiol.1989 1353 447-3457]bacillus species strain 17-1 CGT enzyme is described, Itkor et al [ Itkor P, Tsukagaoshi N and Udaka S;Biochem. Biophys.Res.Commun.1990 166 630-636]bacillus species B1018 CGT enzyme, Schmid et al [ Schmid G, Englbrecht A, Schmid D; proceedings of the Fourth International Symposium onCyclodextrins (Huber O, Szeitli J, Eds.), 198871-76]Bacillus species 1-1 CGT enzymes, Kitamoto et al [ Kitamoto N, Kimura T, KitoY, Ohmiya K;J.Fement.Bioeng.1992 74 345-351]bacillus species KC201 CGT enzyme is described, Sakai et al [ Sakai S, Kubota M, Nakada T, Torigoe K, Ando O and Sugimoto T;J.Jpn.Soc.Starch.Sci.198734 140-147]bacillus stearothermophilus CGT enzyme and Bacillus macerans CGT enzyme are described, Takano et al [ Takano T, Fukuda M, Monma M, Kobayashi S, Kainuma K and Yamane K;J.Bacteriol.1986 166(3)1118-1122]bacillus macerans CGT enzyme, Sin et al [ Sin KA, Nakamura A, Kobayashi K, MasakiH and Uozumi T;Appl.Microbiol.Biotechnol.1991 35 600-605]bacillus ohbensis CGT enzyme, Nitschke et al [ Nitschke L, HeegerK, Bender H and Schultz G; ap (Ap)pl.Microbiol.Biotechnol.1990 33542-546]Bacillus circulans CGTase, Hill et al [ Hill DE, Aldape R and Rozzell JD;Nucleic Acids Res.1990 18 199]bacillus licheniformis CGT enzyme, Tomita et al [ Tomita K, Kaneda M, Kawamura K and Nakanishik;J.Ferm.Bioeng.1993 75(2)89-92]bacillus autolyticus CGT enzyme, Jamuna et al [ Jamuna R, Saswathi N, Shela R and RamakrishnaSV;Appl.Biochem.Biotechnol.1993 43 163-176]bacillus cereus CGTase, Akimaru et al [ Akimaru K, Yagi T and Yamamoto S;J.ferm. Bioeng.1991 71(5)322-328]described is a bacillus coagulans CGT enzyme, SchmidG [ Schmid G;New Trends in Cyclodextrins and. Derivatives(Duchene D，Ed.)，Editions de Sante，Paris，1991，25-54]bacillus firmus CGT enzyme, Abelian et al [ Abelian VA, AdamianMO, Abelian LAA, Balayan AM and Afrikinan EK;Biochememistry(Moscow)1995 60(6)665-669]bacillus halophilus CGT enzymes are described, as well as Kato et al [ Kato T and Horikoshi K;J.Jpn.Soc.Starch Sci.1986 33(2)137-143]bacillus subtilis CGTases are described.

EP 614971 describes brevibacterium CGT enzymes, Haeckel and Bahl [ Haeckel K, Bahl H;FEMS.Microbiol.Lett.1989 60 333-338]clostridium thermosulfurigenes CGT enzymes, Podkovyrov and Zeikus [ Podkovyrov SM, Zeikus JG;J.Bacteriol.1992 174 5400-5405]clostridium thermohydrosulfuricum CGT enzyme is described, JP 7000183 describes Corynebacterium CGT enzyme, Binder et al [ Binder F, Huber O and Bock A;Gene 1986 47 269-277]klebsiella pneumoniae CGT enzymes are described, U.S. Pat. No. 4,317,881Micrococcus CGT enzymes, and Wind et al [ Wind RD, Liebl W, Buitelaar RM, Penninga D, SpreinataA, Dijkhuizen L, Bahl H;Appl.Environ.Microbiol.1995 61(4)1257-1265]thermoanaerobacterium thermosulfurigenes CGT enzymes are described.

CGT enzymes produced by thermoanaerobacter species have been identified by Norman and Jorgensen [ Norman BE, Jorgensen ST;Denpun kagaku19923999-106, and WO 89/03421]) And (5) reporting.

In addition, CGT enzymes derived from thermophilic actinomycetes have been reported [ Abelian VA, AryanKB, Avakian ZG, Melkumyan AG and Afdkian EG;Biochemistry (Moscow)1995 60(10)1223-1229]。

protein engineering has recently been used to modify certain cgtase enzymes to produce specific cyclodextrins selectively to varying degrees.

Other suitable CGT-enzymes for the purposes of the present invention are described in the following documents: hofman et al [ Hofman BE, Bender H, Schultz GE;J.Mol.Biol.1989 209 793-800]and Klein and Schulz [ Klein C, Schulz GE;J.Mol.Biol.1991 217737-750]the tertiary structure of CGT enzyme derived from the strain Bacillus circulans 8, Kubota et al [ Kubota M, Matsuura Y, Sakai S and Katsube Y;Denpun kagaku 199138 141-146]the tertiary structure of CGT enzyme derived from Bacillus stearothermophilus TC-91 was reported, Lawson et al [ Lawson CL, van Montfort R, Strokopotototoov B, RozeboomHJ, Kalk KH, de Vries GE, Penninga D, Dijkhuizen L, and DijkstraBW;J.Mol.Biol.1994 236 590-600]the tertiary structure of CGTase derived from the strain Cyclobacterium 251, Strokopytov et al [ Strokopytov B, PenningaD, Rozebom HJ; kalk KH, Dijkhuizen L and Dijkstra BW;Biochemistry 1995 34 2234-2240]the tertiary structure of the CGTase derived from the strain Cyclobacterium 251, which has been complexed with acarbose, a potent CGTase inhibitor, and Knegtel et al [ Knegtel RMA, Wind RD, Rozeboom HJ,kalk KH, Buitelaar RM, Dijkhuizen L and Dijkstra BW;J.Mol. Biol.1996 256 611-622]the tertiary structure of CGT enzymes derived from Thermoanaerobacterium thermosulfurigenes has been reported. Other CGT-enzymes are described in: in the case of the strain of Cyclobacterium 251 these are Asp229, Glu257 and Asp328, respectively, see Strokopotov et al 1995, in the cited book; variants with improved g-cyclodextrin productivity relative to b-cyclodextrin are described by Sin et al [ Sin, K, Nakamura a, Masaki H, Matsuura Y and Uozumi T;Journal of Biotechnology 1994 32 283-288]and JP-A-5219948. Nakamura et al [ Nakamura A, Haga K and Yamane K;Biochemistry 1994 339929-9936]the effect of substitution of four residues in the active center of the Bacillus species strain 1011 CGTase on substrate binding and cyclization properties is described. In these cgtase variants, phenylalanine at position 183 has been replaced by leucine, tyrosine at position 195 has been replaced by alanine, phenylalanine, leucine, threonine, valine and tryptophan, respectively, phenylalanine at position 259 has been replaced by leucine and phenylalanine at position 283 has been replaced by leucine. Penninga et al [ Penninga D, StrokopotovicB, Rozeboom HJ, Lawson CL, Dijkstra BW, Bergsma J and Dijkhuizen L;Biochemistry 1995 34 3368-3376]the effect of position directed mutations of tyrosine at position 195 of the c.circulans strain 251 CGT enzyme on activity and product selectivity is described. In this publication, four cgtase variants were produced in which the tyrosine at position 195 had been replaced by phenylalanine, tryptophan, leucine and glycine respectively. Fujiware et al [ Fujiwara S, Kakihara H, Sakaguchi K and Imanaka T;J.Bacteriol.1992 174(22)7478-7481]CGTase variants derived from Bacillus stearothermophilus are described in which the tyrosine residue at position 191 (corresponding to position 195, CGTase numbering) has been replaced by phenylalanine, the tryptophan residue at position 254 (corresponding to position 258, CGTase numbering) has been replaced by valine, and the phenylalanine at position 255 (corresponding to position 259, CGTase numbering) has been replaced by phenylalanine and isoleucine, respectivelyAn acid substitution, a threonine residue at position 591 (corresponding to position 598, cgtase numbering) having been substituted with phenylalanine and a tryptophan residue at position 629 (corresponding to position 636, cgtase numbering) having been substituted with phenylalanine. JP-A-7023781 describes CGTase variants derived from Bacillus species 1011 in which the tyrosine residue at position 195 has been replaced by leucine, valine, phenylalanine and isoleucine respectively. JP-A-5244945 describes CGTase variants derived from Bacillus stearothermophilus TC-91 in which the tyrosine residues at positions 222 and 286 (corresponding to positions 195 and 259, CGTase numbering) have been replaced by phenylalanine to improve the relative yield of ｃA-cyclodextrin to b-cyclodextrin. JP-A-5041985 describes CGTase variants derived from Bacillus species #1011 in which the histidine at residue 140 in region A, the histidine at residue 233 in region B and the histidine at residue 327 in region C have been replaced by arginine and asparagine residues, respectively. EP 630,967 describes cgtase variants in which the tyrosine residues at position 211 (corresponding to position 195, cgtase numbering) of the bacillus species 290-3 cgtase, at position 217 (corresponding to position 195, cgtase numbering) of the bacillus species 1-1 cgtase and at position 229 (corresponding to position 195, cgtase numbering) of the bacillus circulans cgtase have been replaced by tryptophan and serine.

Other CGT-enzymes suitable for the purposes of the present invention are the gamma CGT-enzymes, which can be obtained by screening bacteria for secretion of the gamma CGT-enzyme, as described in WO 91/14770.

Other CGT-enzymes suitable for the purposes of the present invention are the enzymes described in WO 96/33267. WO96/33267 describes variants of cgtase which exhibit improved product selectivity and/or reduced product inhibition when compared to the precursor enzyme. Accordingly WO96/33267 provides cgtase variants derived from a precursor cgtase by substitution, insertion and/or deletion of one or more amino acid residues occupying positions close to the substrate.

Other CGT-enzymes suitable for the purposes of the present invention are the enzymes described in WO 99/15633. WO99/15633 describes CGT-enzyme variants which exhibit improved product specificity compared to the wild-type enzyme, wherein one or more amino acid residues corresponding to the following positions have been introduced by substitution and/or insertion (cgtase numbering):

(i) position 47: 47C; 47D; 47E; 47F; 47G; 471; 47K; 47N; 47P; 47R; 47S; 47T; 47V; 47W; or 47Y;

(ii) position 145: 145D; 145H; 1451; 145N; 145Q; or 145V;

(iii) position 146: 146H, 146K; 146L; 146T; 146V; or 146Y;

(iv) position 147: 147C; 147D; 147E; 147N; 147Q;

(v) position 196: 196C; 196E; 196F; 196G; 196H; 1961; 196K; 196L; 196M; 196P; 196Q; 196R; 196T; 196V; or 196W; 196Y and/or

(vi) Position 371: 371C; 371E; 371F; 371H; 3711; 371K; 371L; 371M; 371Q; 371R; 371T; 371V; or 371W.

In this regard, a cgtase variant with improved product specificity is one that is capable of producing an increased proportion of one particular type of cyclodextrin when compared to the wild-type enzyme.

In such cgtase variants, one or more amino acid residues corresponding to the following positions (cgtase numbering) have been introduced by substitution and/or insertion:

(ii) position 145: 145D; 145H; 1451; 145N; 145Q; or 145V;

(iii) position 146: 146H, 146K; 146L; 146T; 146V; or 146Y;

(iv) position 147: 147C; 147D; 147E; 147N; 147Q;

(v) position 196: 196C; 196E; 196F; 196G; 196H; 1961; 196K; 196L; 196M; 196P; 196Q; 196R; 196T; 196V; 196W; or 196Y; and/or

In a preferred embodiment of WO99/15633, there is provided a cgtase variant showing improved product specificity for the production of α -cyclodextrin, in which variant one or more amino acid residues corresponding to the following positions have been introduced by substitution and/or insertion (cgtase numbering):

(i) position 47: 47F; 47K; 47R; 47W; or 47Y;

(ii) position 145: 145D; 145H; 145N; or 145Q;

(iii) position 146: 146H, 146K; 146L; 146T; 146V; or 146Y;

(iv) position 147: 147C; 147D; 147E; 147N; 147Q;

(vi) Position 371: 371C; 371H; 371K; 371R; or 371T.

In another preferred embodiment of WO99/15633, a product specific alternative cgtase variant is provided which shows an improvement for the production of β -cyclodextrin, in which variant another one or more amino acid residues corresponding to the following positions have been introduced by substitution and/or insertion (cgtase numbering):

(i) position 47: 47C; 47D; 47E; 47F; 47G; 471; 47N; 47P; 47S; 47T; 47V; 47W; or 47Y;

(ii) position 145: 145D; 1451; 145N; or 145V;

(iii) position 147: 147E;

(iv) position 196: 196C; 196E; 196F; 196G; 196H; 1961; 196K; 196L; 196M; 196P; 196Q; 196R; 196T; 196V; 196W; or 196Y; and/or

(v) Position 371: 371C; 371E; 371F; 371H; 3711; 371K; 371L; 371M; 371Q; 371R; 371T; 371V; or 371W.

In another preferred embodiment of WO99/15633, a product specific alternative cgtase variant is provided which shows an improvement for the production of γ -cyclodextrin, in which variant another amino acid residue or residues corresponding to the following positions has/have been introduced by substitution and/or insertion (cgtase numbering):

(ii) position 145: 145D; 1451; 145N; or 145V;

(iii) position 147: 147E;

(v) Position 371: 371C; 371E; 371F; 371H; 371K; 371M; 371Q; 371R; 371T; or 371W.

The CGTase variants described in WO99/15633 may be derived from any CGTase found in nature. However, the cgtase variant is preferably derived from a microbial enzyme, preferably a bacterial enzyme, and preferably the cgtase variant is derived from a bacillus strain, a brevibacterium strain, a clostridium strain, a corynebacterium strain, a klebsiella strain, a micrococcus strain, a thermoanaerobacterium strain, or a thermoactinomyces strain. More preferably, the CGT enzyme is derived from a strain of bacillus autolyticus, a strain of bacillus cereus, a strain of bacillus circulans var. Most preferably, the CGTase variant of WO99/15633 is derived from Bacillus sp.1011, Bacillus sp.38-2, Bacillus sp.17-1, Bacillus sp.1-1, Bacillus sp.B 1018, Bacillus circulans strain 8, Bacillus circulans strain 251 or the strain Thermoanaerobacter sp.ATCC 53627, or a mutant or variant thereof.

If the CGTase variant of WO99/15633 is derived from a strain of Cyclobacterium, one or more amino acid residues corresponding to the following positions may be introduced:

(i) position R47: R47C; R47D; R47E; R47F; R47G; r471; R47K; R47N; R47P; R47S; R47T; R47V; R47W; or R47Y;

(ii) position S145: S145D; S145H; s1451; S145N; S145Q; or S145V;

(iii) position S146: S146H, S146K; S146L; S146T; S146V; or S146Y;

(iv) position D147: D147C; D147E; D147N; D147Q;

(v) position D196: D196C; D196E; D196F; D196G; D196H; d1961; DI 96K; D196L; D196M; D196P; D196Q; D196R; D196T; D196V; D196W; or D196Y; and/or

(vi) Position D371; D371C; D371E; D371F; D371H; d3711; D371K; D371L; D371M; D371Q; D371R; D371T; D371V; or D371W.

Preferably, the cgtase variant is derived from the circovirus strain 251, or a mutant or variant thereof.

If the CGTase variant is derived from a strain of Thermoanaerobacterium species, one or more amino acid residues corresponding to the following positions may be introduced:

(i) position K47; K47C; K47D; K47E; K47F; K47G; k471; K47N; K47P; K47R; K47S; K47T; K47V; K47W; or K47Y;

(ii) position S145: S145D; S145H; s1451; S145N; S145Q; or S145V;

(iii) position E146: E146H, E146K; E146L; E146T; E146V; or E146Y;

(iv) position T147: T147C; T147D; T147E; T147N; T147Q;

(v) position D196: D196C; D196E; D196F; D196G; D196H; d1961; D196K; D196L; D196M; D196P; D196Q; D196R; D196T; D196V; D196W; or D196Y; and/or

(vi) Position D371: D371C; D371E; D371F; D371H; d3711; D371K; D371L; D371M; D371Q; D371R; D371T; D371V; or D371W.

Preferably, the CGTase variant is derived from the strain Thermoanaerobacter species ATCC 53627, or a mutant or variant thereof.

Example 1 of WO99/15633 describes the structure of thermothiogenic thermoanaerobacter cgtase variants Asp196His (D196H) and Asp371Arg (D371R) with improved product specificity, wherein site-directed mutagenesis results in an alteration of the hydrogen bond numbering in the sublite of the active site cleft (cleft). The variants are derived from the thermothiogenic thermoanaerobacterium EM1 CGT enzyme (i.e., wild-type) obtained as described by Haeckel and Bahl [ Haeckel, k., and Bahl, H. (1989) FEMS microbiol lett.60, 333-: 611-622(1996)].

In another preferred embodiment of WO99/15633, the cgtase variant comprises one or more of the following amino acid residues (cgtase numbering):

(i)47K/145E/146V/147N；

(ii)47K/145E/146E/147N；

(iii)47K/145D/146R/147D；

(iv)47K/145D/146E/147D；

(v)47K/145E/146V/147N/196H；

(vi)47K/145E/146E/147N/196H；

(vii)47K/145E/146V/147N/196H/371R；

(viii)47K/145E/146E/147N/196H/371R；

(ix)47K/145D/146R/147D/196H；

(x)47K/145D/146E/147D/196H；

(xi) 47K/145D/146R/147D/196H/371R; and/or

(xii)47K/145D/146R/147D/196H/371R.

(xiii)47K/196H；

(xiv)47R/196H

(xv)145E/146V/147N；

(xvi)145E/146E/147N；

(xvii)145D/146R/147D；

(xviii)145D/146E/147D；

(xix)47K/371R；

(xx)47R/371R；

If the CGTase variant is derived from a strain of a Bacillus circulans, one or more of the following amino acid residues may be introduced:

(i)R47K/S145E/S146V/D147N；

(ii)R47K/S145E/S146E/D147N；

(iii)R47K/S145D/S146R；

(iv)R47K/S145D/S146E；

(v)R47K/S145E/S146V/D147N/D196H；

(vi)R47K/S145E/S146E/D147N/D196H；

(vii)R47K/S145E/S146V/D147N/D196H/D371R；

(viii)R47K/S145E/S146E/D147N/D196H/D371R；

(ix)R47K/S145D/S146R/D196H；

(X)R47K/S145D/S146E/D196H；

(Xi)R47K/S145D/S146R/D196H/D371R；

(xii)R47K/S145D/S146R/D196H/D371R.

(xiii)R47K/D196H；

(xiv)S145E/S146V/D147N；

(XV)S145E/S146E/D147N；

(xvi)S145D/S146R；

(xvii)S145D/S146E；

(xviii)R47K/D371R；

If the CGTase variant is derived from a strain of Thermoanaerobacterium species, one or more of the following amino acid residues may be introduced:

(i)S145E/E146V/T147N；

(ii)S145E/T147N；

(iii)S145D/E146R/T147D；

(iv)S145D/T147D；

(V)S145E/E146V/T147N/D196H；

(vi)S145E/T147N/D196H；

(vii)S145E/E146V/T147N/D196H/D371R；

(viii)S145E/T147N/D196H/D371R；

(ix)S145D/E146R/T147D/D196H；

(X)S145D/T147D/D196H；

(xi)S145D/E146R/T147D/D196H/D371R；

(xii)S145D/E146R/T147D/D196H/D371R.

(xiii)S145E/E146V/T147N；

(xiv)S145E/T147N；

(xv)S145D/E146R/T14 D；

(xvi) S145D/T147D; and/or

(xvii)K47R/D371R；

(xviii)K47R/D196H

WO99/43793 describes variants of maltogenic alpha-amylase having CGT-enzymatic activity and CGT-enzyme variants having maltogenic alpha-amylase activity, as well as hybrid enzymes of construction thereof; it shows the required CGT-enzyme properties of the enzyme of the invention. In particular, WO99/43793 describes a polypeptide which:

a) comprises at least 70% of the amino acid sequence of SEQ ID NO: 1 amino acids 1-686 of the same amino acid sequence;

b) including amino acid variants, as compared to SEQ ID NO of WO 99/43793: 1 compared with the domain corresponding to amino acids 40-43, 78-85, 136-139, 173-180, 188-195 or 259-268; and

c) when applied to starch, has the ability to form cyclodextrins.

WO99/47393 also discloses a polypeptide which:

a) contains an amino acid sequence that is at least 70% identical to a parent cyclodextrin glucanotransferase (CGT-enzyme);

b) including amino acid variants, compared to the parent CGT-enzyme, in a nucleic acid sequence corresponding to the amino acid sequence of SEQ ID NO in WO 99/43793: 1, has insertion, substitution or deletion in the domain of amino acids 40-43, 78-85, 136-139, 173-180, 188-195 or 259-268; and

c) when used on starch, has the ability to form linear oligosaccharides.

In more detail, WO99/43793 provides variants of maltogenic alpha-amylases and CGT-enzymes and hybrids, wherein the parent maltogenic alpha-amylase used in the present invention is classified in ec3.2.1.133, preferably the maltogenic alpha-amylase used is described in EP120693, cloned from a bacillus amylase, and wherein the parent CGT-enzyme used is an enzyme classified in ec2.4.1.19, preferably having one or more of the following characteristics:

i) comprises at least 50% of the amino acid sequence of SEQ ID NO: 1, preferably at least 60%;

ii) is encoded by a DNA sequence which hybridizes under the conditions described below to the sequence of SEQ ID NO: 1 or a DNA sequence which hybridizes to a DNA sequence encoding Novamyl present in the bacillus species NCIB 11837; and

iii) the catalytic junction comprises a sequence corresponding to SEQ ID NO: 1 amino acid residues of D228, E256 and D329 in the amino acid sequence shown in amino acids 1-686 of 1.

WO99/43793 describes CGT-enzyme variants which are capable of forming linear oligosaccharides when acting on starch. Such CGT-enzyme variants are disclosed in the corresponding SEQ ID NO: 1, residues 40-43, 78-85, 136-139, 173-180, 189-195 or 259-268. Each variant may be an insertion, deletion or substitution of one or more amino acid residues in the domain. Variants of the parent CGT-enzyme are preferably such that the resulting modified amino acid or amino acid sequence more closely resembles the corresponding amino acid or domain of Novamyl. Thus, a variant may be an insertion or substitution with an amino acid present at the corresponding position of Novamyl, or a deletion of an amino acid not present at the corresponding position of Novamyl.

The CGT-enzyme variant may in particular comprise an insertion in the position corresponding to domain D190-F194 of Novamyl (amino acid sequence listed in SEQ ID NO: 1 of WO 99/43793). Insertions may comprise 3 to 7 amino acids, in particular 4 to 6, for example 5 amino acids. The insert may be DPAGF or an analogue thereof as present in Novamyl, e.g. the first amino acid is negatively charged and the last is aromatic, preferably P, A or G in between. Variants may also include substitutions with a neutral amino acid that is not too large than F, Y or W at the position corresponding to NovamylT189, and other examples of inserts are DAGF, DPGF, DPF, DPAAGF, and DPAAGGF.

Variants in domains 78-85 preferably include deletions of 2-5 amino acids, e.g., 3 or 4, and preferably any aromatic amino acid in domains 83-85 should be deleted or substituted with a non-aromatic amino acid.

The variant in domain 259-268 preferably comprises a deletion of 1-3 amino acids, for example 2. The domains may be modified to correspond to Novamyl.

CGT-enzyme variants may also include variants in other domains, for example in the domains corresponding to amino acids 37-39, 44-45, 135, 140-145, 181-186, 269-273, or 377-383 of Novamyl.

Further variants of the amino acid sequence may be carried out on the second CGT-enzyme, i.e.inserted or substituted for the amino acid present at a given position on the second CGT-enzyme, or they may be made closer to the substrate (8 angstroms less than the substrate, e.g.5 angstroms or 3 angstroms less), as described in WO 96/33267.

The following are some examples (using b.circular counts) based on parent CGT-enzyme variants derived from thermoanaerobacter. Similar variants can be made from other CGT-enzymes.

L194F+^*194aT+^*194bD+^*194cP+^*194dA+^*194eG+D196S

L87H+D89^*+T91G+F91aY+G92^*+G93^*+S94^*+L194F+^*194aT+^*194bD+

^*194cP+^*194dA+^*194eG+D196S

^*194aT+^*194bD+^*194cP+^*194dA+^*194eG+D196S

L87H+D89^*+T91G+F91aY+G92^*+G93^*+S94^*+^*194aT+^*194bD+^*194cP+

^*194dA+^*194eG+D196S

Y260F+L261G+G262D+T263D+N264P+E265G+V266T+^*266aA+^*266bN+

D267H+P268V

^*194aT+^*194bD+^*194cP+^*194dA+^*194eG+D196S+Y260F+L261G+G262D+

T263D+N264P+E265G+V266T+^*266aA+^*266bN+D267H+P268V

WO99/43793 also describes Novamyl variants having the required CGT-enzyme properties of the present invention. When applied to starch, this Novamyl variant also has the ability to form cyclodextrins and has a variant of at least one amino acid residue in the same domain as the CGT-enzyme variant described above. However, the modifications are preferably in the opposite direction, i.e.the resulting modified amino acid or amino acid sequence is made more closely similar to the amino acid or domain of the corresponding CGT-enzyme. Thus, a variant may be an insertion or substitution of an amino acid present at the corresponding position in the CGT-enzyme, or a deletion of an amino acid not present at the corresponding position in the CGT-enzyme. Preferred variants include deletions in domain 190-195, preferably deletion (191-195) and/or substitution of amino acids 188 and/or 189, preferably F188L and/or Y189Y.

Preferred CGT-enzymes for inclusion in the detergent compositions of the invention are the following CGT-enzyme variants of WO99/15633 described in more detail above: CGT enzyme variants with significantly improved product specificity for alpha-cyclodextrin production; CGT-enzyme variants with significantly improved product specificity for the production of beta-cyclodextrin and those with significantly improved product specificity for the production of gamma-cyclodextrin. A more preferred CGTase is the CGTase variant of WO99/15633 with significantly improved product specificity for the production of beta-cyclodextrin.

Such CGT-enzymes are typically present in the detergent compositions of the invention at a level of from 0.0002 wt% to 10 wt%, preferably from 0.001 wt% to 2 wt%, more preferably from 0.001 wt% to 1 wt% pure enzyme of the total detergent composition.

Commercially available CGT-enzymes are the enzyme product sold under the trade name Touzyme by Novo Nordisk A/S, the enzyme product sold under the trade name CGT-enzyme from B.macerans by Amano and the enzyme product sold under the trade name EN301 from B.stearothermophilus by Hayashibara.

Preferred CGT-enzymes for specific applications are alkaline CGT-enzymes, i.e.enzymes having an enzymatic activity of at least 10%, preferably at least 25%, more preferably at least 40% of the maximum activity at a pH of 7-12, preferably 10.5. More preferred CGT-enzymes are those having their maximum activity at a pH of 7-12, preferably 10.5.

In another embodiment of the present invention, the detergent composition comprising a CGT-enzyme and selected from the group consisting of nonionic surfactants, proteases and/or bleaches according to the present invention may further comprise one or more starch binding domains. Such starch binding domains may be incorporated into the detergent compositions of the invention as such or as part of a chimeric CGT-enzyme hybrid enzyme. In fact, the CGT-enzymes of the invention will preferably have or have incorporated therein a Starch Binding Domain (SBD). Enzymes in general, such as amylases, cellulases and xylanases, have a modular structure consisting of a catalytic domain and at least one non-catalytic domain, the functions of which are generally described as the functions of a polysaccharide-binding domain (PBD), a starch-binding domain (SBD), a cellulose-binding domain (CBD) and a xylan-binding domain. These binding domains function to selectively bind substrates to enzymes, and in particular, the primary function of SBD is to bind starch. It has been surprisingly found that detergent compositions of the present invention which additionally comprise one or more SBDs and/or wherein the CGT-enzyme comprises such an SBD will provide more effective starch-containing soil/stain removal. It has also been found that such enzymes can be formulated in a more cost effective manner. Without wishing to be bound by theory, it is believed that such CGT-enzymes will act more specifically on substrates in the wash solution and thus have an increased ability to deposit onto starch-containing stains/soils, which may contribute to improved and/or new performance thereof. Furthermore, it is believed that the incorporation of SBD will fragment the starch surface, resulting in it having a higher hydrolysis rate. Suitable SBDs for use in the present invention are SBDs comprised in the glucoamylase from aspergillus niger (sigma) and the beta-galactosidase from the vacuolar aspergillus (a. awamori). SBD can be recovered and fused by Ford, c. et al at j.cell.biochem. (Suppl.) -14D: 30(1990) and Chen, l. et al in abst.annu.meet.am.soc.microbiol.90: 269(1990) by the methods described in (i).

The enzyme may be of any suitable origin, such as vegetable, animal, bacterial, fungal and yeast origin. The source may also be a mesophilic or a mesophilic (psychrophilic, thermophilic, barotropic, alkalophilic, acidophilic, halophilic, etc.) source. Purified or non-purified forms of these enzymes may be used. At present, it is common practice to modify the native enzyme by protein/genetic engineering techniques for optimal performance in the detergent compositions of the invention. For example, variants can be designed to increase the compatibility of the enzyme with ingredients commonly encountered in such compositions. Alternatively, the variant may be designed to tailor the optimum pH, bleaching or chelant stability, catalytic activity, etc. of the enzyme to a particular cleaning application.

In particular, attention should be focused on oxidation sensitive amino acids in the case of bleach stability and on surface charges for surfactant compatibility. The isoelectric point of such enzymes can be altered by substitution of some charged amino acids, for example increasing the isoelectric point can help to improve compatibility with anionic surfactants. The stability of the enzyme may also be enhanced by forming, for example, additional salt bridges and reinforcing metal binding sites to increase chelator stability.

Nonionic surfactant

The detergent composition of the present invention may comprise a nonionic surfactant as a second essential ingredient, and as described below, preferred nonionic surfactants are selected from polyethylene oxide condensates of alkyl alcohols, amide oxides and alkyl acids and/or mixtures thereof.

The nonionic surfactant is generally present in an amount of from 0.05 to 30% by weight, preferably from 0.1 to 10% by weight, based on the total weight of the composition.

As mentioned above, it has been surprisingly found that detergent compositions of the present invention containing nonionic surfactants synergistically remove starch from fabrics, dishes and other hard surfaces. Without wishing to be bound by theory, it is believed that the nonionic surfactant adsorbs onto the surface of the starch granules, thereby disrupting the starch structure and affecting and preventing the starch reverse process. This disruption of structure increases the ability of the maltogenic alpha-amylase to access the substrate, and furthermore, nonionic surfactants can also be used in the pretreatment process, and thus can reduce the retrogradation of starch. Thus, starch-containing stains/soils can be more easily hydrolyzed by enzymes and synergistic breakdown of starch soils occurs by maltogenic alpha-amylase and nonionic surfactant.

Nonionic surfactants that can be used in the present invention can include essentially any alkoxylated nonionic surfactant, preferably ethoxylated and propoxylated nonionic surfactants. Preferred alkoxylated surfactants may be selected from the group consisting of nonionic condensates of alkyl alcohols, nonionic ethoxylated/propoxylated fatty alcohols, nonionic ethoxylated/propoxylated condensates of propylene glycol, and nonionic ethoxylated condensation products of propylene oxide/ethylene diamine adducts. Highly preferred are nonionic alkoxylated alcohol surfactants which are the products of the condensation of fatty alcohols with 1 to 125 moles of alkylene oxide, especially about 50 or 1 to 15 moles, preferably to 11 moles, especially ethylene oxide and/or propylene oxide, which are highly preferred nonionic surfactants for inclusion in the anhydrous component of the particles of the present invention. The alkyl chain of the aliphatic alcohol can be straight or branched, primary or secondary, and typically contains from about 6 to 22 carbon atoms. Particular preference is given to condensation products of alcohols having an alkyl radical having from 8 to 20 carbon atoms with from 2 to 9 mol, in particular 3,5 or 7 mol, of ethylene oxide per mole of alcohol.

Nonionic surfactants useful herein may also include polyhydroxy fatty acid amides, particularly those having the structure: r²CONR¹Z, wherein R¹Is H, C₁-C₁₈Preferably C₁-C₄Alkyl, 2-hydroxyethyl, 2-hydroxypropyl, ethoxy, propoxy or mixtures thereof, preferably C₁-C₄Alkyl, more preferably C₁Or C₂Alkyl, most preferably C₁Alkyl (i.e., methyl); and R²Is C₅-C₃₁Hydrocarbyl, preferably C₅-C₁₉Or C₇-C₁₉Straight chain alkyl or alkenyl, more preferably straight chain C₉-C₁₇Alkyl or alkenyl, most preferably straight chain C₁₁-C₁₇Alkyl or alkenyl groups, or mixtures thereof; z is a polyhydroxyhydrocarbyl having a linear hydrocarbyl chain with at least 3 hydroxyls directly attached to the chain, or an alkoxylated derivative (preferably ethoxylated or propoxylated) thereof, Z preferably will be derived from a reducing sugar in a reductive amination reaction; more preferably, Z is glyceryl. Preferred nonionic polyhydroxy fatty acid amide surfactants for use in the present invention are C₁₂-C₁₄，C₁₅-C₁₇And/or C₁₆-C₁₈Alkyl N-methylglucamides. It may be particularly preferred that the composition of the invention comprises C₁₂-C₁₈Mixtures of alkyl N-methylglucamides and condensation products of alcohols having an alkyl group containing from 8 to 20 carbon atoms with from 2 to 9 moles, in particular 3,5 or 7 moles, of ethylene oxide per mole of alcohol. The polyhydroxy fatty acid amides may be prepared by any suitable method, one particularly preferred method being described in detail in WO 9206984. Products containing about 95 wt.% polyhydroxy fatty acid amide, small amounts of undesirable impurities, such as fatty acid esters and cyclic amides, and which typically melt above about 80 ℃ can be prepared by this process.

The nonionic surfactants useful in the present invention may also include fatty acid amide surfactants or alkoxylated fatty acid amides, including nonionic surfactants having the general formula: r⁶CON(R⁷)(R⁸) Wherein R is⁶Is an alkyl radical having from 7 to 21 carbon atoms, preferably from 9 to 17 carbon atoms or even from 11 to 13 carbon atoms, R⁷And R⁸Each independently selected from hydrogen and C_1-4Alkyl radical, C_1-4Hydroxyalkyl, and- (C)₂H₄O)_xH, where x is 1 to 11, preferably 1 to 7, where R may be preferred⁷And R⁸In contrast, x of one is 1 or 2 and x of one is 3 to 11 or preferably 3 to 7.

Nonionic surfactants useful in the present invention may also include fatty acid alkyl esters, including those having the general formula: r⁹COO(R¹⁰) Wherein R is⁹Is an alkyl radical having from 7 to 21 carbon atoms, preferably from 9 to 17 carbon atoms or even from 11 to 13 carbon atoms, R¹⁰Is C₁-C₄Alkyl radical, C₁-C₄Hydroxyalkyl, or- (C)₂H₄O)_xH, wherein x is 1 to 11, preferably 1 to 7, more preferably 1 to 5, wherein R may be preferred¹⁰Is methyl or ethyl.

Nonionic surfactants useful in the present invention may also include alkyl polysaccharides such as those disclosed in U.S. patent 4565647 issued to llenod on 21.1.1986, having hydrophobic groups containing 6 to 30 carbon atoms and polysaccharides such as polyglycosides, hydrophilic groups containing 1.3 to 10 saccharide units.

Preferred alkylpolyglycosides have the formula:

R²O(C_nH_2nO)_t(sugar base)_x

Wherein R is²Selected from the group consisting of alkyl, alkylphenyl, hydroxyalkyl, hydroxyalkylphenyl, and mixtures thereof, wherein the alkyl group contains from 10 to 18 carbon atoms; n is 2 or 3; t is 0-10 and x is 1.3-8. The glycosyl is preferably derived from glucose.

Also suitable as nonionic surfactants for the purposes of the present invention are semi-polar nonionic surfactants: semi-polar nonionic surfactants are a particular class of nonionic surfactants which include, alkyl moieties containing from about 10 to about 18 carbon atoms and two-sided active agents which include, water-soluble amine oxides containing an alkyl moiety containing from about 10 to about 18 carbon atoms and two moieties selected from the group consisting of alkyl and hydroxyalkyl containing from about 1 to about 3 carbon atoms; a water soluble phosphine oxide containing one alkyl moiety of from about 10 to about 18 carbon atoms and two moieties selected from the group consisting of alkyl and hydroxyalkyl containing from about 1 to about 3 carbon atoms; water-soluble sulfoxides containing one alkyl moiety of from about 10 to about 18 carbon atoms and one moiety selected from the group consisting of alkyl and hydroxyalkyl moieties of from about 1 to about 3 carbon atoms.

Semi-polar nonionic detergent surfactants include amine oxide surfactants having the general formula:

wherein R is³Is an alkyl, hydroxyalkyl, or alkylphenyl group, or mixtures thereof, containing from about 8 to about 22 carbon atoms; r⁴Is an alkylene or hydroxyalkylene group containing from about 2 to about 3 carbon atoms or mixtures thereof; x is 0 to about 3; each R is⁵Is an alkyl or hydroxyalkyl group containing from about 1 to about 3 carbon atoms or a polyoxyalkylene group containing from about 1 to about 3 ethylene oxide groups. R⁵The groups may be linked to each other, such as through an oxygen or nitrogen atom, to form a cyclic structure.

These amine oxide surfactants include in particular C₁₀-C₁₈Alkyl dimethyl amine oxide and C₈-C₁₂Alkoxyethyl dihydroxyethylamine oxide.

When included in the present invention, the cleaner compositions of the present invention generally comprise from 0.2 wt% to about 15 wt%, preferably from about 1 wt% to about 10 wt%, of such semi-polar nonionic surfactants.

Also suitable for use as nonionic surfactants for the purposes of the present invention are cosurfactants selected from primary or tertiary amines. Primary amines suitable for use in the present invention include R₁NH₂Wherein R is₁Is C₆-C₁₂Is preferably C₆-C₁₀Alkyl chain of (2) or R₄X(CH₂)_nX is-O-, C (O) NH-or-NH-, R₄Is C₆-C₁₂Alkyl chain, n is 1-5, preferably 3, R₁The alkyl chain may be straight or branched and may be interrupted by up to 12, preferably less than 5, ethylene oxide moieties.

Preferred amines according to the above formula of the present invention are n-alkylamines, and amines suitable for use in the present invention may be selected from the group consisting of 1-hexylamine, 1-octylamine, 1-decylamine and laurylamine. Other preferred primary amines include C₈-C₁₀Oxypropylamine, octyloxypropylamine, 2-ethylhexyl oxypropylamine, laurylamidopropylamine and amidopropylamine.

Tertiary amines suitable for use in the present invention include tertiary amines having the general formula: r₁R₂R₃N, wherein R₁And R₂Is C₁-C₈Alkyl chain or

R₃Is C₆-C₁₂Preference is given toC₆-C₁₀Alkyl chain of (2) or R₃Is R₄X(CH₂)_nWherein X is-O-, C (O) NH-or-NH-, R₄Is C₄-C₁₂N is 1-5, preferably 2-3, R₅Is hydrogen or C₁-C₂Alkyl, x is 1-6.

R₃And R₄May be straight-chain or branched, R₃The alkyl chain may be interrupted by up to 12, preferably less than 5, ethylene oxide moieties.

Preferred tertiary amines are R₁R₂R₃N, wherein R₁Is C₆-C₁₂Alkyl chain, R₂And R₃Is C₁-C₃Alkyl or

Wherein R is₅Is hydrogen or methyl, and x is 1-2.

Also preferred are amidoamines having the formula:

wherein R is₁Is C₆-C₁₂An alkyl group; n is 2 to 4, preferably n is 3; r₂And R₃Is C₁-C₄。

The most preferred amines of the present invention include 1-octylamine, 1-hexylamine, 1-decylamine, 1-dodecylamine, C_8-10Oxypropylamine, N-coco 1-3 diaminopropane, cocoalkyl dimethylamine, lauryl di (hydroxyethyl) amine, coco di (hydroxyethyl) amine, 2 moles propoxylated laurylamine, 2 moles propoxylated octylamine, lauryl amidopropyl dimethylamine, C_8-10Amidopropyldimethylamine and C₁₀Amidopropyl dimethylamine.

The most preferred amines for use in the compositions of the present invention are 1-hexylamine, 1-octylamine, 1-decylamine, 1-dodecylamine. Particularly desirable are n-dodecyl dimethylamine and diethoxy cocoyl alkylamine and 7 moles of ethoxylated oleyl amine, laurylamidopropylamine and cocoylamidopropylamine.

Protease enzyme

The second component of the detergent composition of the invention may be a protease. As mentioned above, starch-containing stains and soils also include a number of protein components. Without wishing to be bound by theory, it is believed that the protease will hydrolyze the proteins containing this complex stain and thereby result in synergistic removal of this stain/soil along with the maltose alpha-amylase. In addition, the hydrolyzed complex stains/soils have a lower molecular weight in the wash solution, which therefore results in the hydrolyzed complex stains no longer being deposited on the surface to be cleaned.

Suitable proteases are subtilisin BPN and BPN' strains from bacillus subtilis and bacillus licheniformis (b.licheniformis). A suitable protease is obtained from Bacillus, having maximum activity over the entire pH range of 8-12, developed and marketed by Novo Industries A/S of Denmark, hereinafter referred to as "Novo", and by ESPERASE^And (5) selling. The preparation of this enzyme and isoenzymes is described in GB1,243,784 of Novo. Other suitable proteases include ALCALASE from Novo^，DURAZYM^，SAVINASE^(protease Subtilisin 309 from Bacillus subtilis) and MAXATASE from Gist-Brocades^，MAXACAL^，PROPERASE^And MAXAPEM^(from protein engineered MAXACAL). Also suitable for the present invention are the proteases described in patent applications EP251446 and WO91/06637, the protease BLAP described in WO91/02792^And variants thereof as described in WO 95/23221. See WO93/18140A from Novo corporation for a high pH protease from Bacillus NCIMB 40338. Comprises protease, one or more other enzymes, and a composition comprisingEnzymatic detergents of reversible protease inhibitors are described in WO92/03529A from Novo. When desired, the method described in Procter can be used&WO95/07791 to Gamble has proteases with reduced adsorption and increased hydrolysis. Recombinant trypsin-like proteases suitable for use in the detergents of the invention are described in WO94/25583 from Novo. Other suitable proteases are described in EP516200 from Unilever.

Proteolytic enzymes also include modified bacterial serine proteases such as those described in EP251446 filed on 28.4.1987 (especially variant Y217L described on pages 17, 24 and 98), which is referred to herein as "protease B", and those mentioned on 29.10.1986 by Venegas in european patent application 199,404, which refers to a modified bacterial serine protease referred to herein as "protease a". Suitably, the so-called "protease C" in the present invention is a variant of an alkaline serine protease from Bacillus, in which lysine is substituted for arginine at position 27, tyrosine for valine at position 104, serine for asparagine at position 123 and alanine for threonine at position 274. Protease C is described in WO 91/06637. Genetically modified variants, in particular of protease C, are also encompassed by the invention.

Preferred proteases referred to as "protease D" are carbonyl hydrolase variants having an amino acid sequence not found in nature, derived from a precursor carbonyl hydrolase by substitution of a number of amino acid residues at the position corresponding to position +76 in the carbonyl hydrolase with different amino acids, preferably in combination with one or more amino acid residue positions corresponding to those selected from the group consisting of +99, +101, +103, +104, +107, +123, +27, +105, +109, +126, +128, +135, +156, +166, +195, +197, +204, +206, +210, +216, +217, +218, +222, +260, +265 and/or +274, according to Bacillus amyloliquefaciens subtilisin numbering, as described in WO95/10591 and WO 95/10592. The variant of "protease D" preferably has an amino acid substitution combination of 76/103/104, more preferably has a substitution combination of N76D/S103A/V1041. Also suitable is a carbonyl hydrolase variant of the protease described in WO95/10591, the amino acid sequence of which is derived by substitution of a number of amino acid residues at the position of the precursor enzyme corresponding to +210 with one or more of the following residues: +33, +62, +67, +76, +100, +101, +103, +104, +107, +128, +129, +130, +132, +135, +156, +158, +164, +166, +167, +170, +209, +215, +217, +218, and +222, where the numbering positions correspond to naturally occurring subtilisin from Bacillus amyloliquefaciens, or to equivalent amino acid residues in other carbonyl hydrolases or subtilisin, such as Bacillus subtilis subtilisin (co-pending patent application published as WO 98/55634).

More preferably the protease is a polysubstituted protease variant. These protease variants comprise a combination of an amino acid residue substitution at position 103 corresponding to Bacillus amyloliquefaciens subtilisin with another naturally occurring amino acid residue and an amino acid residue substitution at the following positions corresponding to Bacillus amyloliquefaciens subtilisin:

1,3,4,8,9, 10, 12, 13, 16, 17, 18, 19, 20, 21, 22, 24, 27, 33, 37, 38, 42, 43, 48, 55, 57, 58, 61, 62, 68, 72, 75, 76, 77, 78, 79, 86, 87, 89, 97, 98, 99, 101, 102, 104, 106, 107, 109, 111, 114, 116, 117, 119, 121, 123, 126, 128, 130, 131, 133, 134, 137, 140, 141, 142, 146, 147, 158, 159, 160, 166, 167, 170, 173, 174, 177, 181, 182, 183, 184, 185, 188, 192, 194, 198, 203, 204, 205, 206, 209, 210, 211, 212, 213, 214, 215, 216, 217, 218, 222, 224, 227, 228, 230, 232, 236, 237, 238, 240, 242, 243, 244, 245, 246, 247, 248, 249, 251, 252, 253, 254, 255, 256, 257, 258, 259, 260, 261, 262, 263, 265, 268, 269, 270, 271, 272, 274 and 275; wherein when said protease variant comprises amino acid residue substitutions at positions corresponding to positions 103 and 76, there is also a substitution of an amino acid residue at one or more amino acid residue positions not corresponding to positions 27, 99, 101, 104, 107, 109, 123, 128, 166, 204, 206, 210, 216, 217, 218, 222, 260, 265 or 274 of Bacillus amyloliquefaciens subtilisin and/or a multiply substituted protease variant comprising an amino acid residue substitution with another naturally occurring amino acid residue at one or more positions 62, 212, 230, 232, 252 or 257 corresponding to Bacillus amyloliquefaciens subtilisin, as described in WO99/20727, WO99/20726 and WO99/20723, all filed by Procter & Gamble, 1998 at 23 and 10. Preferred multi-substituted protease variants have an amino acid substitution combination of 101/103/104/159/232/236/245/248/252, more preferably an amino acid substitution combination of 101G/103A/1041/159D/232V/236H/245R/248D/252K, as numbered in accordance with Bacillus amyloliquefaciens subtilisin.

More preferred proteases for the purposes of the present invention are the proteolytic enzymes sold under the trade name Savinase by Novo Nordisk A/S, "protease B" variants with Y217L substitution described in EP251446, "protease D" variants with N76D/S103A/V1041 substitution combinations and proteases with 101G/103A/1041/159D/232V/236H/245R/248D/252K amino acid substitution combinations described in WO99/20727, WO99/20726 and WO 99/20723.

Proteases are generally incorporated into detergent compositions in amounts of from 0.0001% to 2%, preferably from 0.0001% to 0.1%, more preferably from 0.001% to 0.05% pure enzyme by weight of the detergent composition.

Bleaching agent

The second element of the detergent composition of the invention may be a bleaching agent. Without wishing to be bound by theory, it is believed that the oxidation of the starchy material by the bleaching agent dissolves the starchy material and, therefore, allows the starchy material to be more easily removed and caused to no longer deposit on the surface to be cleaned. Thus, the compositions of the present invention, which also contain a bleaching agent, provide synergistic removal of starch-containing stains and soils, and have improved whiteness maintenance and soil cleaning ability when formulated as laundry compositions.

Preferred bleaching agents for use in the detergent compositions of the present invention are percarbonate in combination with a bleach activator selected from nonanoyloxybenzene sulphonate (NOBS), hydroxybenzenesulphonate of N-nonanoyl-6-aminocaproic acid (NACA-OBS), and/or Tetraacetylethylenediamine (TAED). Also preferred is what is known as [ Mn (Bcycalam) Cl₂]The bleaching agent of (1).

Suitable bleaching agents for the purposes of the present invention include hydrogen peroxide, PB1, PB4 and percarbonate having a particle size of 400-800 μm. These bleach components may include one or more oxygen bleaches, and, depending on the choice of bleach, one or more bleach activators. When present, oxygen bleaching compounds are typically present in amounts of from 0.1% to 30%, preferably from 1% to 20% by weight of the detergent composition.

The bleach component for use herein may be any bleach useful in detergent compositions, including oxygen bleaches as well as other bleaches known in the art, and bleaches suitable for the present invention may be activated or unactivated bleaches.

One type of oxygen bleaching agent that may be used comprises percarboxylic acid bleaching agents and salts thereof. Suitable examples of such agents include magnesium monoperoxyphthalate hexahydrate, magnesium m-chloroperbenzoate, magnesium 4-nonylamino-4-oxoperoxybutyrate and magnesium diperoxydodecanedioate. These bleaching agents are disclosed in U.S. Pat. No. 4,483,781, U.S. patent application 740,446, European patent application 0,133,354 and U.S. Pat. No. 4,412,934. Highly preferred bleaching agents also include 6-nonylamino-6-oxaperoxy hexanoic acid, described in U.S. Pat. No. 4,634,551.

Another bleaching agent that may be used includes halogen bleaches. Examples of hypochlorite bleaches include, for example, trichloroisocyanuric acid and sodium and potassium dichloroisocyanurate, and N-chloro and N-bromo alkane sulfonamides. Such materials are generally added in amounts of 0.5 to 10 wt%, preferably 1 to 5 wt%, based on the weight of the finished product.

The hydrogen peroxide releasing agent may be used in combination with a bleach activator, such as Tetraacetylethylenediamine (TAED), nonanoyloxybenzenesulfonate (NOBS, described in U.S. Pat. No. 4,412,934), 3, 5-trimethylhexanoloxybenzenesulfonate (ISONOBS, described in EP120,591) or Pentaacetylglucose (PAG) or hydroxybenzenesulfonate of N-nonanoyl-6-aminocaproic acid (NACA-OBS, described in WO 94/28106), which perhydrolyzes to form a peracid as the active bleaching species, resulting in an increased bleaching effect. Also suitable activators are acylated citrate esters, as disclosed in EP624154, and unsymmetrical acyclic imide bleach activators having the general formula:

wherein R is₁Is C₇-C₁₃Linear or branched, saturated or unsaturated alkyl, R₂Is C₁-C₈Linear or branched, saturated or unsaturated alkyl, R₃Is C₁-C₄A linear or branched saturated or unsaturated alkyl group. In the detergent compositions of the present invention, those bleach activators are generally used in an amount of 0.1 to 10%, preferably 0.5 to 5%, by weight of the detergent composition.

Suitable bleaching agents for use in the detergent compositions of the present invention, including peroxyacids, and bleaching systems comprising a bleach activator and a peroxygen bleaching compound are described in our co-pending applications WO95/10592, WO97/00937, WO95/27772, WO95/27773, WO95/27774 and WO 95/27775.

The presence of hydrogen peroxide may also be achieved by adding an enzyme system (i.e. the enzyme and its substrate) capable of generating hydrogen peroxide at the beginning or during the washing and/or rinsing operation. Such an enzyme system is disclosed in EP 537381.

Metal-containing catalysts for bleaching compositions include cobalt-containing catalysts, such as pentamine cobalt (III) acetate salts, and manganese-containing catalystsAgents, such as those described in EPA 549271; EPA 549272; EPA 458397; US5,246,621; EPA 458398; those described in US5,194,416 and US5,114,611. Bleaching compositions comprising a peroxygen compound, a manganese-containing bleach catalyst and a chelating agent are described in patent application 94870206.3. The bleaching compound may be catalysed by a manganese compound. Such compounds are well known in the art, for example, manganese-based catalysts are disclosed in U.S. Pat. nos. 5,246,621, 5,244,594; us patent 5,194,416; us patent 5,114,606; and european patent application publication nos. 549,271a1, 549,272a1, 544,440a2, and 544490a 1; preferred examples of these catalysts include Mn^IV ₂(u-O)₃(1, 4, 7-trimethyl-1, 4, 7-triazacyclononane)₂(PF₆)₂，Mn^III ₂(u-O)₁(u-OAc)₂(1, 4, 7-trimethyl-1, 4, 7-triazacyclononane)₂(ClO₄)₂，Mn^IV ₄(u-O)₆(1, 4, 7-triazacyclononane)₄(ClO₄)₄，Mn^IIIMn^IV ₄(u-O)₁(u-OAc)₂- (1, 4, 7-trimethyl-1, 4, 7-triazacyclononane)₂(ClO₄)₃，Mn^IV(1, 4, 7-trimethyl-1, 4, 7-triazacyclononane) (OCH₃)₃(PF₆) And mixtures thereof.

More preferred for use in the present invention are transition metal bleach catalysts which are complexes of a transition metal and a cross-linked bridged macromolecular polycyclic ligand, as in Procter&Those described in Gamble patent applications WO98/39405, WO98/39406 and WO 98/39098. Most preferred are those having the formula [ Mn (Bcycalam) Cl₂]The structure of the manganese complex bleaching catalyst is as follows:

"Bcycam", (5, 12-dimethyl-1, 5,8, 12-tetraaza-bicyclo [6.6.2] hexadecane or 5, 12-diethyl-1, 5,8, 12-tetraaza-bicyclo [6.6.2] hexadecane). Such transition metal bleach catalysts may be prepared according to the method in patent application WO98/39335 to Procter & Gamble or according to j.amer.chem.soc., (1990), 112, 8604. These bleach catalysts may generally be included in the detergent compositions of the present invention in an amount of from 0.0007 to 0.07%, preferably from 0.005 to 0.05% by weight of the detergent composition.

Bleaching agents other than oxygen bleaching agents are also known in the art and may be used in the present invention. One particularly preferred non-oxygen bleaching agent comprises a photoactivated bleaching agent such as a sulfonated zinc and/or aluminum phthalocyanine. These materials can be deposited on the substrate during the washing process. In the presence of oxygen, upon irradiation with light, such as by sun drying by hanging the garment outdoors, the zinc phthalocyanine sulfonate is activated and thus bleaches the substrate. Preferred zinc phthalocyanine and photoactivated bleaching processes are described in U.S. Pat. No. 4,033,718. Typically, the detergent composition will comprise from about 0.025% to about 1.25% by weight of the zinc phthalocyanine sulfonate.

Also suitable as bleach species for the purposes of the present invention are colour safe bleach boosters which may be used in conjunction with a peroxygen source in a bleaching composition. Bleach boosters are generally present in detergent compositions in amounts of from 0.01% to 10%, more preferably from 0.05% to 5% by weight of the composition. Bleach boosters for inclusion in the detergent compositions of the present invention include zwitterionic imines, anionic iminium polyions having a net negative charge of from about-1 to about-3, and mixtures thereof.

Suitable imine bleach boosters of the present invention include those having the structure:

wherein R is¹-R⁴May be hydrogen or unsubstituted or substituted radicals selected from the group consisting of phenyl, aryl, heterocycle, alkyl and cycloalkyl, with the exception of at least one R¹-R⁴Including anionically charged moieties.

Preferred bleach boosters are negatively charged moieties bound to the imine nitrogen, as described in WO 97/10323. Also preferred are tricyclic oxaziridinium compounds as described in US5,710,116 and bleach boosters as described in WO98/16614, which may be prepared according to the methods described in WO97/10323 and/or WO 98/16614.

Detergent component

The detergent composition of the present invention will preferably comprise another enzyme selected from lipase, alpha-amylase, cyclomaltodextrin glucanotransferase and/or amyloglucosidase.

In a preferred embodiment, the present invention relates to laundry and/or fabric care compositions comprising a maltogenic alpha-amylase and a detergent ingredient selected from the group consisting of nonionic surfactants, proteases and/or bleaches (examples 1-17). In a second embodiment, the present invention relates to dishwashing or household cleaning compositions (examples 18-23).

The compositions of the present invention may be formulated, for example, as hand and machine dishwashing compositions, hand and machine laundry detergent compositions including laundry additive compositions and compositions suitable for soaking and/or pretreating soiled fabrics, rinse agents incorporating fabric softener compositions, and compositions for use in ordinary household hard surface cleaning operations. When formulated into a composition for use in a hand dishwashing process, the compositions of the present invention preferably comprise a surfactant and preferably further detergent components selected from organic polymers, suds enhancers, group II metal ions, solvents, hydrotropes and additional enzymes.

When formulated as a composition suitable for use in a washing machine washing process, the compositions of the present invention preferably comprise both a surfactant and a builder compound and additionally comprise one or more detergent components preferably selected from organic polymers, bleaches, additional enzymes, suds suppressors, dispersants, lime-based soap dispersants, soil suspension and anti-redeposition agents and preservatives. The laundry composition may also comprise a softening agent as an additional detergent component. When formulated into laundry detergent compositions, such compositions comprising detergent ingredients selected from nonionic surfactants, proteases and/or bleaches, and maltogenic alpha-amylase enzymes provide starch-containing stain removal, whiteness maintenance, and soil cleaning benefits.

The compositions of the present invention may also be used as detergent additive products. Such additive products are intended to supplement or boost the performance of conventional detergent compositions.

The detergent composition of the present invention may be a liquid, paste, gel, bar, tablet, spray, foam, powder or granule. Granular compositions may also be in "compact" form, and liquid compositions may also be in "concentrated" form. If desired, the laundry detergent compositions of the present invention may have a density, as measured at 20 ℃, in the range of 400-. The "compact" form of the compositions of the invention is best reflected in terms of density and composition by the amount of inorganic filler salt; inorganic filler salts are conventional ingredients in detergent compositions in powder form; in conventional detergent compositions, the filler salt is present in an amount of from 17 to 35 wt% based on the total weight of the composition. In the compacted composition, the filler salt is present in an amount of no more than 15 wt%, preferably no more than 10 wt%, most preferably no more than 5 wt% of the total weight of the composition. Inorganic filler salts, as have the meaning in the compositions of the present invention, are selected from the group consisting of the sulfates and chlorides of alkali and alkaline earth metals. A preferred filler salt is sodium sulfate. The liquid detergent compositions of the present invention may also be in "concentrated form", in which case they will contain lower amounts of water than conventional liquid detergents. Generally, the water content of the concentrated liquid detergent is preferably less than 40%, more preferably less than 30%, most preferably less than 20% by weight of the detergent composition.

Suitable detergent compounds for use in the present invention are selected from the compounds described below.

Surfactant system

In addition to nonionic surfactants, the detergent compositions of the present invention may comprise a surfactant system wherein the surfactant may be selected from anionic and/or cationic and/or amphoteric and/or zwitterionic surfactants.

The surfactant is typically present in an amount of 0.1% to 60% by weight. More preferably, the level of incorporation is from 1% to 35% by weight, most preferably from 1% to 30% by weight of the detergent composition of the present invention.

The surfactant is preferably formulated so as to be compatible with the enzyme components present in the composition. In liquid or gel compositions, the surfactant is most preferably formulated so as to increase, or at least not decrease, the stability of any enzyme in these compositions.

Anionic surfactant:

suitable anionic surfactants which may be used are linear alkylbenzene sulphonate, alkyl ester sulphonate surfactants which include C₈-C₂₀Linear esters of carboxylic acids (i.e.fatty acids) are prepared according to The method of "The Journal of The American Oil Chemists Society", 52, (1975), page 323-329 with gaseous SO₃And (3) sulfonation. Suitable starting materials will include natural fatty materials such as those derived from tallow, palm oil, and the like.

Preferred alkyl ester sulfonate surfactants, particularly for laundry applications, include alkyl ester sulfonate surfactants having the formula:

wherein R is³Is C₈-C₂₀A hydrocarbyl group, preferably an alkyl group, or a combination thereof, R⁴Is C₁-C₆A hydrocarbyl group, preferably an alkyl group, or a combination thereof, M is with an alkyl ester sulfonic acidThe salt forms the cation of the water-soluble salt. Suitable salt-forming cations include metals, such as sodium, potassium, and lithium, and substituted or unsubstituted ammonium cations, such as monoethanolamine, diethanolamine, and triethanolamine. Preferably, R³Is C₁₀-C₁₆Alkyl radical, R⁴Is methyl, ethyl or isopropyl. Particularly preferred is where R³Is C₁₀-C₁₆Alkyl methyl ester sulfonates.

Other suitable anionic surfactants include alkyl sulfate surfactants of the formula ROSO₃Water-soluble salts or acids of M, wherein R is preferably C₁₀-C₂₄Hydrocarbyl, preferably alkyl or having C₁₀-C₂₀Hydroxyalkyl of the alkyl component, more preferably C₁₂-C₁₈Alkyl or hydroxyalkyl, M is H or a cation, for example, an alkali metal cation (e.g., sodium, potassium, lithium), or ammonium or substituted ammonium, such as methyl, dimethyl, and trimethyl ammonium cations and quaternary ammonium cations, such as tetramethyl ammonium and dimethyl piperidine cations and quaternary ammonium cations derived from alkylamines such as ethylamine, diethylamine, triethylamine, and mixtures thereof, and the like. Generally, for lower wash temperatures (e.g., less than about 50℃.), C₁₂-C₁₆Alkyl chains are preferred, while for higher wash temperatures (e.g., above about 50℃.), C is preferred_16-18An alkyl chain.

Other anionic surfactants useful for detersive purposes can also be included in the detergent compositions of the present invention. These may include salts of soaps (including, for example, sodium, potassium, ammonium and substituted ammonium salts such as mono-, di-and triethanolamine salts), C₈-C₂₂Salts of primary or secondary alkanes, C₈-C₂₄Olefin sulfonates, sulfonate polycarboxylic acids prepared by sulfonation of the pyrolysis product of alkaline earth metal citrates, e.g. the sulfonate polycarboxylic acids described in British patent Specification 1,082,179, C₈-C₂₄Alkyl polyglycol ether sulfates (containing up to 10 moles of ethylene oxide); alkyl glyceryl sulfonate, fatty acyl glyceryl sulfonate, fatty oil-based glyceryl sulfate, alkylphenol ethylene oxide ether sulfateParaffin sulphonates, alkyl phosphates, isethionates, e.g. acyl isethionates, N-acyl taurates, alkyl succinates and sulphosuccinates, sulphosuccinates monoesters (in particular saturated and unsaturated C's)₁₂-C₁₈Monoesters) and sulfosuccinic acid diesters (in particular saturated and unsaturated C)₆-C₁₂Diesters), acyl sarcosinates, alkyl polysaccharide sulfates, alkyl polyglucoside sulfates (nonionic nonsulfated compounds described below), branched primary alkyl sulfates, and alkyl polyethoxy carboxylates, such as those of the formula RO (CH)₂CH₂O)_k-CH₂COO^-M⁺Wherein R is C₈-C₂₂Alkyl, k is an integer from 1 to 10, and M is a cation forming a soluble salt. Resin acids and hydrogenated resin acids are also suitable, such as rosin, hydrogenated rosin, and resin acids and hydrogenated resin acids present in or derived from tall oil.

Further examples are described in "Surface Active Agents and Detergents" (volumes I and II, Schwartz, Perryand Berch). Many such surfactants are also widely disclosed in U.S. Pat. No. 3,929,678 issued to Laughlin et al, at 12/30 of 1975, column 23, line 58-column 29, line 23 (which is incorporated herein by reference).

When included herein, the laundry detergent compositions of the present invention generally comprise from about 1 wt% to about 40 wt%, preferably from about 3 wt% to about 20 wt%, of such ionic surfactants.

Highly preferred anionic surfactants include alkyl alkoxylated sulfate type surfactants, where it is of the type having RO (A)_mSO₃Water soluble salts or acids of M, wherein R is unsubstituted C₁₀-C₂₄Alkyl or having C₁₀-C₂₄Hydroxyalkyl of alkyl components, preferably C₁₂-C₂₀Alkyl or hydroxyalkyl, more preferably C₁₂-C₁₈Alkyl or hydroxyalkyl, A is an ethoxy or propoxy unit, M is greater than 0, typically between about 0.5 and about 6, more preferably between about 0.5 and about 3, M is H or a cation,it can be, for example, a metal cation (e.g., sodium, potassium, lithium, calcium, magnesium, etc.), an ammonium or substituted ammonium cation. Alkyl ethoxylated sulfates as well as alkyl propoxylated sulfates are contemplated in the present invention. Specific examples of substituted ammonium cations include methyl, dimethyl, trimethyl-ammonium cations and quaternary ammonium cations such as tetramethyl-ammonium and dimethyl piperdine cations and those derived from, for example, ethylamine, diethylamine, triethylamine, mixtures thereof, and the like. An exemplary surfactant is C₁₂-C₁₈Alkyl polyethoxylate (1.0) sulfate (C)₁₂-C₁₈E(1.0)M)、C₁₂-C₁₈Alkyl polyethoxylate (2.25) sulfate (C)₁₂-C₁₈E(2.25)M)、C₁₂-C₁₈Alkyl polyethoxylate (3.0) sulfate (C)₁₂-C₁₈E (3.0) M) and C₁₂-C₁₈Alkyl polyethoxylate (4.0) sulfate (C)₁₂-C₁₈E (4.0) M), where M may conveniently be selected from sodium and potassium.

Cationic surfactant:

cationic surfactants suitable for use in the detergent compositions of the present invention are those having one long chain hydrocarbyl group. Examples of such cationic surfactants include ammonium surfactants, such as alkyltrimethylammonium halides, and those having the formula:

[R²(OR³)_y][R⁴(OR³)_y]₂R⁵N⁺X^-

wherein R is²Is an alkyl or alkylbenzyl radical having from about 8 to about 18 carbon atoms in the alkyl chain, each R³Is selected from-CH₂CH₂-，-CH₂CH(CH₃)-，-CH₂CH(CH₂OH)-，-CH₂CH₂CH₂-, and mixtures thereof; each R⁴Is selected from C₁-C₄Alkyl radical, C₁-C₄Hydroxyalkyl radical, by linkingIs connected with two R⁴Benzyl cyclic structure formed by the radicals, -CH₂CHOH-CHOHCOR⁶CHOHCH₂OH, wherein R⁶Is any hexose or hexose polymer having a molecular weight below about 1000, and is hydrogen when y is other than 0; r⁵And R⁴Is the same as or is wherein R²Plus R⁵Alkyl chains having a total number of carbon atoms of no more than about 18; each y is from 0 to about 10, the total number of y values being from 0 to about 15; x is any compatible anion.

Quaternary ammonium surfactants suitable for the present invention have the following formula (I):

formula I

Wherein R1 is a short chain alkyl (C6-C10) or alkylamidoalkyl of formula (11):

formula II

y is 2 to 4, preferably 3;

wherein R2 is H or C1-C3 alkyl,

wherein x is 0 to 4, preferably 0 to 2, most preferably 0,

wherein R3, R4 and R5 are identical or different and can be short-chain alkyl radicals (C1-C3) or alkoxylated alkyl radicals of the formula III,

wherein X^-As counter-ion, preference is given to halides, such as chloride or methylsulfate.

Formula III

R6 is C₁-C₄And z is 1 or 2.

Preferred quaternary ammonium surfactants are those as defined in formula I wherein

R₁Is C₈、C₁₀Or a mixture thereof, x ═ o,

R₃、R₄＝CH₃and R₅＝CH₂CH₂OH。

Highly preferred cationic surfactants for use in the compositions of the present invention are water soluble quaternary ammonium compounds having the formula:

R₁R₂R₃R₄N⁺X^-(i)

wherein R is₁Is C₈-C₁₆Alkyl radical, each R₂、R₃And R₄Independently is C₁-C₄Alkyl radical, C₁-C₄Hydroxyalkyl, benzyl, and- (C)₂H₄O)_xH, wherein X is 2-5 and X is an anion. R₂、R₃Or R₄At most one of which should be benzyl. For R₁Has a preferred alkyl chain length of C₁₂-C₁₅In particular where the alkyl group is a mixture of chain lengths derived from coconut or palm kernel fat or synthesised by olefin polymerisation or oxo alcohol synthesis. Is preferably used for R₂、R₃And R₄Is methyl and hydroxyethyl and the anion X may be selected from halide, methosulfate, acetate and phosphate ions. Examples of quaternary ammonium compounds of formula (i) suitable for use in the present invention are:

coconut trimethyl ammonium chloride or bromide;

coconut methyl dihydroxyethyl ammonium chloride or bromide;

decyl triethyl ammonium chloride;

decyl dimethyl hydroxyethyl ammonium chloride or bromide;

C_12-15dimethylhydroxyethylammonium chloride or bromide;

coconut dimethyl hydroxyethyl ammonium chloride or bromide;

myristyltrimethylammonium methyl sulfate;

lauryl dimethyl benzyl ammonium chloride or bromide;

lauryl dimethyl (ethoxy)₄Ammonium chloride or bromide;

choline esters (compounds of formula (i) wherein R₁Is composed of

CH₂CH₂OC(O)C_12-14Alkyl radical, R₂R₃R₄Is methyl);

dialkyl imidazolines [ compounds of formula (i) ].

Other cationic surfactants useful in the present invention are also described in U.S. patent 4,228,044 issued to Cambre at 10/14 1980 and european patent application EP000,224.

Typical cationic fabric softening compositions comprise a water-insoluble quaternary ammonium fabric softening active or its corresponding amine precursor, most commonly ammonium chloride or methyl sulphate with a double long alkyl chain is used.

Among the preferred cationic softeners are those listed below:

1) ditalloxyldimethylammonium chloride (DTDMAC);

2) dihydrogenated tallow dimethyl ammonium chloride;

3) dihydrogenated tallow dimethyl ammonium methyl sulfate;

4) distearyldimethylammonium chloride;

5) dioleyl dimethyl ammonium chloride;

6) dipalmityl hydroxyethyl methylammonium chloride;

7) stearyl benzyl dimethyl ammonium chloride;

8) tallow trimethyl ammonium chloride;

9) hydrogenated tallow trimethyl ammonium chloride;

10)C_12-14alkyl hydroxyethyl dimethyl ammonium chloride;

11)C_12-18alkyl bis hydroxyethyl methylammonium chloride;

12) bis (stearoyloxyethyl) dimethylammonium chloride (DSOEDMAC);

13) di (tallow-oxyethyl) dimethylammonium chloride;

14) ditallol imidazoline methosulfate;

15)1- (2-tallowamidoethyl) -2-tallowimidazoline methylsulfate.

Biodegradable quaternary ammonium compounds have been presented as alternatives to the traditionally used di-long alkyl chain ammonium chlorides and methyl sulfates. Such quaternary ammonium compounds contain long chain alk (en) yl groups interrupted by functional groups, such as carboxyl groups. Such materials and fabric softening compositions comprising them are disclosed in ｃA number of publications, such as EP-A-0,040,562 and EP-A-0,239,910.

The quaternary ammonium compounds and amine precursors of the present invention have the following formula (I) or (II):

or

Wherein,

q is selected from the group consisting of-O-C (O) -, -O-, -NR⁴-C(O)-，-C(O)NR⁴-；

R¹Is (CH)₂)_n-Q-T²Or T³；

R²Is (CH)₂)_m-Q-T⁴Or T⁵Or R³；

R³Is C₁-C₄Alkyl or C₁-C₄Hydroxyalkyl or H;

R⁴is H or C₁-C₄Alkyl or C₁-C₄A hydroxyalkyl group;

T¹，T²，T³，T⁴，T⁵independently is C₁₁-C₂₂An alkyl or alkenyl group;

n and m are integers from 1 to 4; and

X^-is an anion compatible with the softener. Non-limiting examples of anions compatible with the softening agent include chloride or methyl sulfate.

Alkyl, or alkenyl, chains T¹，T²，T³，T⁴，T⁵Must contain at least 11 carbon atoms, preferably at least 16 carbon atoms. The chain may be straight or branched. Tallow is a convenient and inexpensive source of long chain alkyl and alkenyl materials. Compounds having the following characteristics are particularly preferred, T¹、T²、T³、T⁴、T⁵Represents a mixture of long chain substances typically used for tallow.

Specific examples of quaternary ammonium compounds suitable for use in the aqueous fabric softening compositions of the present invention include:

1) n, N-bis (tallow-oxyethyl) -N, N-dimethylammonium chloride;

2) n, N-di (tallow-oxyethyl) -N-methyl, N- (2-hydroxyethyl) ammonium methyl sulfate;

3) n, N-bis (2-tallow-oxy-2-oxoethyl) -N, N-dimethylammonium chloride;

4) n, N-bis (2-tallow-oxy-ethylcarbonyl-oxyethyl) -N, N-dimethylammonium chloride; 5) n-bis (2-tallow-oxo-2-ethyl) -N- (2-tallow-oxo-2-oxoethyl) -N, N-dimethylammonium chloride;

6) n, N-tris (tallow-oxyethyl) -N-methylammonium chloride;

7) n- (2-tallow-oxo-2-oxoethyl) -N- (tallow-N, N-dimethyl) ammonium chloride; and

8)1, 2-ditalloyl-oxy-3-trimethylammoniopropane chloride; and mixtures of any of the above.

When included herein, the detergent compositions of the present invention generally comprise from 0.2 wt% to about 25 wt%, preferably from about 1 wt% to about 8 wt%, of such cationic surfactants.

Amphoteric surfactant:

amphoteric surfactants are also suitable for use in the compositions of the present invention. These surfactants can be broadly described as aliphatic derivatives of secondary or tertiary amines, or aliphatic derivatives of heterocyclic secondary and tertiary amines in which the aliphatic radical can be straight or branched chain. One of the aliphatic substituents contains at least about 8 carbon atoms, typically from about 8 to about 18 carbon atoms, and at least one contains an anionic water-solubilizing group, e.g., carboxyl, sulfonic acid, sulfuric acid. See, for example, U.S. Pat. No. 3,929,678 to Laughlin et al, column 19, lines 18-35, at 12/30 of 1975.

When included herein, the detergent compositions of the present invention generally comprise from 0.2% to about 15%, preferably from about 1% to about 10%, by weight of such amphoteric surfactants.

Zwitterionic surfacesActive agent(s):

zwitterionic surfactants are also suitable for use in detergent compositions. These surfactants can be broadly described as aliphatic derivatives of secondary or tertiary amines, or aliphatic derivatives of heterocyclic secondary and tertiary amines, or derivatives of quaternary ammonium, quaternary phosphonium, or tertiary sulfonium compounds. See, for example, U.S. patent No. 3,929,678 issued to Laughlin et al at 12/30 of 1975, column 19, line 38 to column 22, line 48.

When included herein, the detergent compositions of the present invention generally comprise from 0.2% to about 15%, preferably from about 1% to about 10%, by weight of such zwitterionic surfactants.

Conventional detergent enzymes

In addition to CGT-enzymes, the detergent compositions of the present invention may comprise one or more enzymes capable of providing cleaning performance, fabric care and/or sanitizing action. The enzymes include the following: cellulases, hemicellulases, peroxidases, proteases, glucoamylases, amylases, mannanases, xyloglucanases, xylanases, lipases, phospholipases, esterases, cutinases, pectinases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, malanases, beta-glucanases, arabinosidases, hyaluronidase, chondroitinase, laccase, or mixtures thereof.

Preferably, the detergent compositions of the present invention will comprise an enzyme selected from lipase, alpha-amylase, maltogenic alpha-amylase and/or amyloglucosidase. Indeed, it has now been found that the combination of a CGT-enzyme with an alpha-amylase, maltogenic alpha-amylase and/or amyloglucosidase enzyme in a detergent composition of the invention provides improved removal of raw and/or reverse starch. In addition, the most commonly encountered stains in laundry, dishwashing and hard surface cleaning typically include large amounts of protein and triglyceride compounds. In particular, it has been found that starch materials are often associated with lipid compounds. Thus, it has now been found that further combinations with lipases in the detergent compositions of the invention provide enhanced removal of such complex stains.

Thus, detergent compositions containing such enzyme combinations enhance starch-containing stain and soil removal and, when formulated as laundry compositions, have enhanced whiteness maintenance and soil cleaning capabilities.

Alpha-amylase

As noted above, the detergent compositions of the present invention will preferably comprise an alpha-amylase. Alpha-amylases suitable for the purposes of the present invention are described in the literature as follows: WO94/02597, Novo Nordisk A/S, published on month 2 and 3 of 1994, describes cleaning compositions incorporating mutant amylases, also described in WO95/10603, Novo Nordisk A/S, published on month 4 and 20 of 1995. Other amylases known to be useful in cleaning compositions include alpha-and beta-amylases, alpha-amylases being known in the art and including those disclosed in U.S. patent 5,003,257; EP252,666; WO 9100353; FR2,676,456; EP285,123; EP525,610; EP368,341; and those in british patent specification 1,296,839 (Novo).

Other suitable amylases are stability-enhanced amylases, described in WO94/18314, published in 1994, 8/18 and in WO96/05295 of Genencor, published in 1996, 2/22, and amylase variants with additional modifications in the intermediary matrix, obtained from Novo Nordisk A/S, disclosed in WO9510603, published in 95, 4. Also suitable are the amylases described in EP277216, WO95/26397 and WO96/23873 (all of which are Novo Nordisk). An example of a commercial alpha-amylase product is Purafect Oxam from Genencor^And Termamyl from Novo Nordisk A/S, Denmark^，Ban^，Fungamyl^And Duramyl^. WO95/26397 describes other suitable amylases: alpha-amylase characterized by using Phadebas in the temperature range of 25-55 ℃ and the pH range of 8-10^Specific activity ratio of Termamyl when measured in an alpha-amylase activity assay^Is at least 25% higher. Preferred are variants of the above enzymes described in WO96/23873 (NovoNordisk). Preferably, the variants are those that exhibit increased thermostability, more preferably wherein at least one amino acid residue equivalent to F180, R181, G182, T183, G184 or K185 has been deleted from the parent alpha-amylase. Particularly preferred are those with improved thermal stability comprising R181^*+G182^*Or T183^*+G184^*A deletion variant. Other amylases with improved properties in terms of degree of activity and their combination of thermostability with a higher degree of activity are described in WO 95/35382. Further suitable amylases are H mutant alpha-amylases showing improved stability, described in WO98/26078 of Genencor.

The alpha-amylase is incorporated into the detergent composition in an amount of from 0.0001% to 2%, preferably from 0.00018% to 0.06%, more preferably from 0.00024% to 0.048% pure enzyme by weight of the composition.

Maltogenic alpha-amylases

Further preferred enzymes are maltogenic alpha-amylases of the IUPAC class EC3.2.1.133 which hydrolyze 1, 4-alpha-D-glycosidic bonds in glycans such that consecutive alpha-maltose units are removed from the non-reducing end. Suitable maltogenic alpha-amylases are described in EP120639, WO99/43793 and WO 99/43794. Commercially available maltogenic alpha-amylases are the enzyme products sold under the trade name Novamyl by Novo Nordisk A/S.

Such maltogenic alpha-amylases are typically comprised in the detergent compositions of the invention at a level of from 0.0002 wt% to 10 wt%, preferably from 0.001 wt% to 2 wt%, more preferably from 0.001 wt% to 1 wt% pure enzyme of the total detergent composition.

Amyloglucosidase

Also preferred is an amyloglucosidase enzyme classified by IUPAC as ec3.2.1.3, which is glucose 1, 4-alpha-glucosidase; also known as "glucoamylase, gamma-amylase, lysosomal-alpha-glucosidase, acid maltase or exo-1, 4-alpha-glucosidase", the system name 1, 4-alpha-D-glucan hydrolase. Suitable amyloglucosidases are described in WO92/00381, WO00/04136 and WO 99/28448. Commercially available amyloglucosidase is the enzyme product sold by MAPS under the tradename PALKODEX; an enzyme product sold by Novo Nordisk A/S as AMG300L, an enzyme product sold by Genencor as Optimax 7525 (enzyme combination including amyloglucosidase) and Spezyme. Further commercially available amyloglucosidase enzymes are those from Aspergillus niger, available from the following companies: ambazyme, Amano, Boehringer, Fluka, Sigma, Aldomax, Genzyme, Nagase, UOP. Also suitable are amyloglucosidase from Aspergillus species from the company Biocatalysts or Danisco, and amyloglucosidase from Rhizopus nigeri from the company Nagase; aminoglucosidase from Rhizopus niveus (Rhizopus niveus) from Amano, ICN, Seikagaku, Aminoglucosidase from Rhizopus oryzae from Enzyme Development Co-operation.

Lipases are likewise preferred. Suitable lipases include, as disclosed in UK patent 1,372,034, those prepared from microorganisms of the Pseudomonas species, such as Pseudomonas stutzeri ATCC 19.154. Suitable lipases include those which exhibit a positive immunological cross-reaction to the lipase antibody, prepared from the microorganism Pseudomonas fluorescens IAM 1057. Such lipases are available from Amano Pharmaceutical Co.Ltd., Nagoya, Japan under the trade name Lipase P "Amano", hereinafter "Amano-P". Other suitable commercial lipases include Amano-CES, a lipase from Chromobacterium viscosum, e.g., Lipotium NRRLB 3673, a variant of Chromobacterium viscosum from Toyo Jozoco, Tagata, Japan; chromobacterium viscosum lipase from Biochemical Corp, USA and Disoynth, Netherlands, and lipase from Pseudomonas gladioli. Particularly suitable lipases are, for example, M1Lipase^RAnd Lipomax^R(Gist-Brocades) and Lipolase^RAnd LipolaseUltra^R(Novo)，Which is considered to be very effective when used in combination with the composition of the present invention. Also suitable are the lipolytic enzymes described in EP258068, WO92/05249 and WO95/22615 of Novo Nordisk and in WO9403578, WO95/35381 and WO96/00292 of Unilever.

Also suitable are cutinases [ EC3.1.1.50], which can be considered as a special class of lipases, in other words lipases which do not require interfacial activation. The incorporation of cutinases into detergent compositions has been described, for example, in WO-A88/09367 (Genencor); WO90/09446(plant genetic System) and WO94/14963 and WO94/14964 (Unilever).

The lipase and/or cutinase are typically incorporated into the detergent composition at a level of from 0.0001% to 2% pure enzyme by weight of the detergent composition.

Cellulases useful in the present invention include bacterial or fungal cellulases. Preferably, they have an optimum pH of 5 to 12 and a specific activity of 50 CEVU/mg or more (cellulose viscosity unit). Suitable cellulases are disclosed in U.S. Pat. Nos. 4,435,307, J61078384, and WO96/02653 to Barbesgord et al, which disclose fungal cellulases prepared from the genera Humicola insolens, Trichoderma, Rhizopus, and Mucor, respectively. EP739982 describes cellulases isolated from novel bacillus species. Suitable cellulases are also disclosed in GB-A-2.075.028; GB-A-2.095.275; DE-OS-2.247.832 and WO 95/26398.

Examples of such cellulases are cellulases (Humicola grayata variant thermoidea) prepared from a strain of Humicola insolens, in particular the strain DSM 1800.

Other suitable cellulases are cellulases derived from humicola insolens having a molecular weight of about 50KDa, an isoelectric point of 5.5, and comprising 415 amino acids; and an approximately 43kD endoglucanase derived from humicola insolens, DSM 1800, exhibiting cellulase activity; the amino acid sequence of a preferred endoglucanase component is disclosed in PCT patent application WO 91/17243. Equally suitable cellulases are the EGIII cellulases from Trichoderma longibrachiatum as described in WO94/21801, filed 9/29 of 1994, Genencor, a particularly suitable cellulase being a cellulase with colour care. Examples of such cellulases are described in European patent application 91202879.2(Novo) filed on 6.11.1991. Carezyme and Celluzyme (Novo Nordisk A/S) are particularly useful. See also WO91/17244 and WO 91/21801. Other suitable cellulases for use in fabric care and/or cleaning properties are described in WO96/34092, WO96/17994 and WO 95/24471.

The cellulase is typically incorporated into the detergent composition at a level of from 0.0001% to 2% pure enzyme by weight of the detergent composition.

Peroxidases are used in combination with oxygen sources such as percarbonates, perborates, persulfates, hydrogen peroxide, etc., and with phenolic substrates as bleach-enhancing molecules. They are used for "solution bleaching", i.e. for preventing dyes or pigments removed from a substrate during a washing operation from migrating to other substrates in the washing solution. Peroxidases are known in the art and include, for example, horseradish peroxidase, ligninase and haloperoxidase, such as chloro-and bromo-peroxidase. Detergent compositions containing peroxidase enzymes are disclosed, for example, in PCT International applications WO89/099813, WO89/09813 and European patent application EP91202882.6 filed 11/6/1991 and EP96870013.8 filed 19962/20. Also suitable are laccases.

Typically, the enhancer is included in an amount of 0.1% to 5% by weight of the total composition. Preferred enhancers are substituted phenothiazines and phenoxazines 10-phenothiazinepropionic acid (PPT), 10-ethylphenothiazine-4-carboxylic acid (EPC), 10-phenoxazinepropionic acid (POP) and 10-methylphenoxazine (described in WO 94/12621) and substituted syringyl esters (C)₃-C₅Substituted alkyl syringyl esters) and phenol. Sodium percarbonate or perborate are preferred sources of hydrogen peroxide.

The peroxidase enzyme is typically incorporated into the detergent composition at a level of from 0.0001% to 2% pure enzyme by weight of the detergent composition.

The above-mentioned enzymes may be of any suitable origin, such as plant, animal, bacterial, fungal and yeast origin. The source may also be a mesophilic or a xenotropic (psychrophilic, thermophilic, barotropic, alkalophilic, acidophilic, halophilic, etc.) source. Purified or non-purified forms of these enzymes may be used. At present, it is common practice to modify the native enzyme by protein/genetic engineering techniques for optimal performance in the detergent compositions of the invention. For example, variants can be designed to increase the compatibility of the enzyme with the ingredients typically encountered in such compositions. Alternatively, the variants may be designed to tailor the optimum pH of the enzyme, bleaching or chelant stability, catalytic activity, etc. to a particular cleaning application.

In particular, attention should be focused on oxidation sensitive amino acids in the case of bleach stability and surface charges for surfactant compatibility. The isoelectric point of such enzymes can be altered by substitution of some charged amino acids, for example increasing the isoelectric point can help to improve compatibility with anionic surfactants. The stability of the enzyme may also be enhanced by the formation of, for example, additional salt bridges and enhanced calcium binding sites which may increase the stability of the chelator. Special care must be taken with cellulases, since most cellulases have an isolated binding domain (CBD). The properties of this enzyme can be altered by modifying these domains.

The enzymes may be added as separate individual components (pellets, granules, stabilized liquids, etc. containing one enzyme) or as a mixture of two or more enzymes (e.g., composite granules).

Other suitable detergent ingredients that may be added are enzymatic oxidation scavengers, described in co-pending european patent application 92870018.6 filed 1/31 1992. An example of such an enzymatic oxidation scavenger is ethoxylated tetraethylene polyamine.

A number of enzymatic materials and means for incorporating them into synthetic detergent compositions are also disclosed in WO9307263A and WO9307260A by Genencor International, WO8908694 by Novo, and US3,553,139 by McCarty et al, 1971, 5.1. Additionally, enzymes are disclosed in US4,507,219 issued to Place et al, 7/18 1978, 3/26, 4,101,457,1985, Hughes. Enzyme materials useful in liquid detergent formulations, and the relevant disclosure of their incorporation into such formulations, are disclosed in U.S.4,261,868 issued to Hora et al on 4/14 of 1981. Enzymes for detergents can be stabilized by various methods. Methods for enzyme stabilization are disclosed and exemplified in U.S. Pat. No. 3,600,319 issued to Gedge et al at 8.17.1971, EP199,405 and EP200,586 of Venegas published at 10.29.1986. Enzyme stabilization systems are also described, for example, in US3,519,570. A useful Bacillus strain AC 13 from which proteases, xylanases and cellulases are obtainable is described in WO9401532A from the company Novo. Color care and fabric care effects

Methods of providing a color care effect may also be included. Examples of these methods are metal catalysts for color retention. Such metal catalysts are described in co-pending european patent application 92870181.2. Dye fixatives, polyolefin dispersions for wrinkle resistance and water absorption enhancement, perfumes and amino functional polymers for color care treatment (PCT/US97/16546) and perfume substantivity are also further examples of color care/fabric care technology, which is described in co-pending patent application 96870140.9 filed 11/7/1996.

Fabric softeners may also be incorporated into the detergent compositions of the present invention. These agents may be of inorganic or organic type. Inorganic softeners are exemplified by smectite clays in GB-a-1400898 and USP 5,019,292. Organic fabric softeners include water-insoluble tertiary amines (as disclosed in GB-A1514276 and EP-BO 011340) together with a single C₁₂-C₁₄Combinations of quaternary ammonium salts (as disclosed in EP-B-0026527 and EP-B-0026528), and bis-long chain amides (as disclosed in EP-B-0242919). Other useful organic components of fabric softening systems include high molecular weight polyethylene oxidesSubstantially, those disclosed in EP-A-0299575 and 0313146.

The amount of smectite is generally between 2% and 20% by weight, more preferably between 5% and 15% by weight, which is added to the remaining components of the formulation as dry mix components. Organic fabric softeners such as water insoluble tertiary amines or di-long chain amide materials are incorporated in amounts of 0.5% to 5% by weight, typically 1% to 3% by weight, while high molecular weight polyethylene oxide materials and water soluble cationic materials are added in amounts of 0.1% to 2% by weight, typically 0.15% to 1.5% by weight. These materials are typically added to the spray-dried portion of the composition, although in some cases it may be more convenient to add them as dry mixed granules, or spray them as a molten liquid onto the other solid components of the composition.

Builder system

The compositions of the present invention may additionally comprise a builder system. Any conventional builder system is suitable for use herein, including aluminosilicate materials, silicates, polycarboxylates, materials of alkyl or alkenyl succinic acids and fatty acids, such as ethylenediamine tetraacetate, diethylenetriamine pentamethylene acetate, metal ion sequestrants, such as aminopolyphosphonates, particularly ethylenediamine tetramethylene phosphonic acid and diethylenetriamine pentamethylene phosphonic acid. Phosphate builders may also be used herein.

Further suitable builders can be inorganic ion exchange materials, typically inorganic hydrated aluminosilicate materials, more particularly hydrated synthetic zeolites such as hydrated zeolite A, X, B, HS or MAP.

Another suitable inorganic builder substance is a layered silicate, for example SKS-6 (Hoechst). SKS-6 is a sodium silicate (Na)₂Si₂O₅) A crystalline layered silicate of composition.

Suitable polycarboxylates containing one carboxy group include lactic acid, glycolic acid and ether derivatives thereof as disclosed in belgian patents 831,368, 821,369 and 821,370. Polycarboxylates containing two carboxy groups include the water-soluble salts of succinic, malonic, (ethylenedioxy) acetoacetic, maleic, dihydroxyacetic, tartaric, hydroxymalonic and fumaric acids, and the ether carboxylates described in German patents 2,446,686 and 2,446,687 and U.S. Pat. No. 3,935,257 and the sulfinyl carboxylates described in Belgian patent 840,623. Polycarboxylates containing three carboxy groups include, inter alia, water soluble citrates, itaconates and citraconates and succinate derivatives such as the carboxymethyl oxysuccinate described in british patent 1,379,241, the lactyloxy succinate described in dutch application 7205873, and oxypolycarboxylate materials such as the 2-oxa-1, 1, 3-propane tricarboxylate described in british patent 1,387,447.

Polycarboxylates containing four carboxy groups include oxydisuccinate, 1, 1,2, 2-ethanedicarboxylic acid, 1, 1,3, 3-propanetetracarboxylic acid and 1, 1,2, 3-propanetetracarboxylic acid, as disclosed in British patent No. 1,261,829. Polycarboxylates containing sulfo substituents include the sulfosuccinate derivatives disclosed in british patents 1,398,421 and 1,398,422 and U.S. patent 3,936,448 and the sulfonated pyrolysed citrates described in british patent 1,082,179, while polycarboxylates containing phosphorus substituents are disclosed in british patent 1,439,000.

Alicyclic and heterocyclic polycarboxylates include cyclopentane-cis, cis-tetracarboxylic acid salts, cyclopentadiene pentacarboxylate, 2, 3,4, 5-tetrahydrofuran-cis, cis-tetracarboxylic acid salts, 2, 5-tetrahydrofuran-cis-dicarboxylate salts, 2, 2,5, 5-tetrahydrofuran tetracarboxylate salts, 1,3, 4,5, 6-hexane-hexacarboxylate salts and carboxymethyl derivatives of polyols such as sorbitol, mannitol and xylitol. Aromatic polycarboxylates include mellitic acid, pyromellitic acid and phthalic acid derivatives as disclosed in British patent 1,425,343.

Among the above, preferred polycarboxylates are hydroxycarboxylic acid salts containing up to three carboxyl groups per molecule, more particularly citrates.

Preferred builder systems for use in the compositions of the present invention comprise a mixture of a water-insoluble aluminosilicate builder, such as zeolite A or layered silicate (SKS-6), and a water-soluble carboxylate chelating agent, such as citric acid. Other preferred builder systems include mixtures of water-insoluble aluminosilicate builders, such as zeolite a, and water-soluble carboxylate chelating agents, such as citric acid. Preferred builder systems for use in the liquid detergent compositions of the present invention are soaps and polycarboxylates.

Other builder materials that may form part of the builder system for the particulate composition include inorganic materials such as alkali metal carbonates, bicarbonates, silicates, and organic materials such as organic phosphonates, amino polyalkylene phosphonates and amino polycarboxylates.

Other suitable water-soluble organic salts are homo-or co-polymeric acids or salts thereof, wherein the polycarboxylic acid contains at least two carboxyl groups separated from each other by not more than two carbon atoms. Polymers of this type are disclosed in GB-A1,596,756. Examples of such salts are polyacrylates of molecular weight Mw2000-5000 and copolymers thereof with maleic anhydride having a molecular weight of 20,000-70,000, in particular about 40,000.

Builder salts are typically included in amounts of from 5% to 80% by weight of the composition, preferably from 10% to 70% by weight, most typically from 30% to 60% by weight.

Chelating agents

The detergent compositions of the present invention may also optionally comprise one or more iron and/or manganese chelating agents. Such chelating agents may be selected from the group consisting of aminocarboxylates, aminophosphonates, polyfunctionally-substituted aromatic chelating agents and mixtures thereof, all as hereinafter defined. Without wishing to be bound by theory, it is believed that the effectiveness of these materials is due in part to their superior ability to remove iron and manganese ions from the wash liquor by forming dissolved chelates.

Aminocarboxylates which can be used as optional chelating agents include ethylenediaminetetraacetate, N-hydroxyethylenediaminetriacetate, nitrilotriacetate, ethylenediaminetetrapropionate, triethylenetetraminehexaacetate, diethylenetriaminepentaacetate and ethanoldiglycinate, alkali metal, ammonium and substituted ammonium salts thereof, and mixtures thereof.

Aminophosphonates are also suitable for use as chelating agents in the compositions of the present invention when at least a low total phosphorus content is permitted in the detergent composition, and include ethylenediaminetetra (methylene phosphate), such as DEQUEST. Preferably, these amino phosphonates do not contain alkyl or alkenyl groups with more than about 6 carbon atoms.

Polyfunctionally substituted aromatic chelating agents may also be used in the compositions of the present invention. See U.S. Pat. No. 3,812,044 issued to Connor et al, 5, 21, 1974. Such compounds in acid form are preferably dihydroxydisulfobenzenes, such as 1, 2-dihydroxy-3, 5-disulfobenzene.

The preferred chelating agent for use in the present invention is ethylenediamine disuccinate ("EDDS"), particularly the [ S, S ] isomer, as described in U.S. patent 4,704,233 issued to Hartman and Perkins at 11/3 1987.

The compositions of the present invention may also contain a water-soluble methylglycine diacetic acid (MGDA) salt (in its acid form) as a chelating agent or co-builder, for example, together with insoluble builders such as zeolites, layered silicates and the like.

If used, these chelants will generally be included in the detergent compositions of the present invention in amounts of from about 0.1% to about 15% by weight of the composition. More preferably, if used, these chelating agents will generally be included in the composition in an amount of about 0.1% to 3.0% by weight of the composition. Suds suppressor

Another optional ingredient is a suds suppressor, such as a silicone and silica-silicone mixture. Siloxanes can generally be represented by alkylated polysiloxane materials, while silica is generally used in the form of fine powders, such as silica aerogels and xerogels, as well as various types of hydrophobic silica. These materials may be incorporated in particulate form, wherein the suds suppressor is advantageously incorporated in a slow release manner into a water-soluble or water-dispersible, substantially non-surface active detergent-impermeable carrier. Alternatively, the suds suppressor can be dissolved or dispersed in a liquid carrier and applied by spraying onto one or more of the other components.

Preferred silicone foam control agents are disclosed in U.S. patent 3933672 to Bartollota et al. Other particularly useful suds suppressors are self-emulsifying silicone suds suppressors described in German patent application DTOS2646126 published on 28.4.1977. An example of such a compound is DC-544, sold by Dow Corning, which is a siloxane-ethylene glycol copolymer. Particularly preferred foam control agents are mixtures comprising silicone oils and 2-alkyl alkanols. Suitable 2-alkyl alkanols are the 2-butyl-octanols commercially available under the trade name Iso fol 12R.

This suds suppressor system is described in co-pending European patent application 92870174.7 filed 11/10 1992.

Particularly preferred silicone suds controlling agents are described in co-pending European patent application N92201649.8. The composition may include a non-porous silica, such as Aerosil^RA combination of siloxane/silica mixtures is used.

The suds suppressors described above are generally used in amounts of from 0.001% to 2% by weight, preferably from 0.01% to 1% by weight, based on the weight of the composition.

Other Components

Other components for detergent compositions may be used, such as soil suspending agents, soil release agents, optical brighteners, abrasives, bactericides, tarnish inhibitors, coloring agents, and/or encapsulated or non-encapsulated perfumes.

Particularly suitable encapsulating materials are water-soluble capsules consisting of a polysaccharide and a polyol matrix, such as those described in GB1,464,616. Other suitable water-soluble encapsulating materials include dextrins derived from ungelatinized starch acid-esters of substituted dicarboxylic acids, such as those described in US3,455,838. These acid-ester dextrins are preferably prepared from starches such as waxy corn, waxy sorghum, sago, tapioca and potato. Suitable examples of the encapsulating material include N-Lok manufactured by national starch company. The N-Lok encapsulating material consists of modified corn starch and glucose. Starch can be modified by the addition of monofunctional substituted groups, such as octenyl succinic anhydride.

Anti-redeposition and soil suspension agents suitable for use in the present invention include cellulose derivatives such as methyl cellulose, carboxymethyl cellulose and hydroxyethyl cellulose, and homo-or co-polymeric polycarboxylic acids or salts thereof. Such polymers include the polyacrylates and copolymers of maleic anhydride and acrylic acid mentioned above as builders, and copolymers of maleic anhydride and ethylene, methyl vinyl ether or methacrylic acid, with maleic anhydride constituting at least 20 mol% of the copolymer. These materials are generally used in amounts of 0.5% to 10%, more preferably 0.75% to 8%, most preferably 1% to 6% by weight of the composition.

Preferred optical brighteners are anionic in nature, examples being 4, 4' -bis (2-ethanolamino-4-anilino-s-triazin-6-ylamino) stilbene-2: disodium 2 ' -disulfonate, disodium 4,4 ' -bis (2-morpholino-4-anilino-s-triazine-6-ylamino-stilbene-2: 2 ' -disulfonate, disodium 4,4 ' -bis (2, 4-dianilino-s-triazine-6-ylamino) stilbene-2: 2 ' -disulfonate, disodium 4,4 ' -bis (2, 4-dianilino-s-triazine-6-ylamino-stilbene-2 ' -sulfonate, disodium 4,4 ' -bis (2-anilino-4- (N-methyl-N-2-hydroxyethylamino) -s-triazine-6-ylamino) stilbene-2, 2 ' -disulfonate, 4,4 ' -bis (4-phenyl-2, 1, 3-triazol-2-yl) -stilbene-2, 2 ' -disulfonic acid disodium, 4,4 ' -bis (2 anilino-4- (1-methyl-2-hydroxyethylamino) -s-triazin-6-ylamino) stilbene-2, 2 ' -disulfonic acid disodium, 2 (stilbene-4 "- (naphtho 1 ', 2 ': 4, 5) -1, 2, 3-triazol-2" -sulfonic acid sodium and 4,4 ' -bis (2-thiostyryl) biphenyl highly preferred brighteners are the specific brighteners disclosed in EP 753567.

Other useful polymeric materials are polyethylene glycols, particularly those having a molecular weight of 1000-. These are used in amounts of 0.20% to 5% by weight, more preferably 0.25% to 2.5% by weight. These polymers and the previously mentioned homo-or copolymeric polycarboxylates are useful for enhancing whiteness maintenance, fabric dirt deposition, and cleaning performance on clay, protein and oxidizable soils in the presence of transition metal impurities.

Soil release agents useful in the present invention are typically copolymers or terpolymers of terephthalic acid and ethylene glycol and/or propylene glycol units in various arrangements. Examples of such polymers are disclosed in commonly assigned US4116885, US4711730 and european published patent application 0272033. A particularly preferred polymer corresponds to EP-A-0272033, which has the formulｃA:

(CH₃(PEG)₄₃)_0.75(POH)_0.25[T-PO)_2.8(T-PEG)_0.4]T(POH)_0.25((PEG)₄₃CH₃)_0.75

wherein PEG is- (OC)₂H₄) O-, PO is (OC)₃H₆O), T is (pcOC)₆H₄CO)。

Also very useful are modified polyesters, such as dimethyl terephthalate, dimethyl sulfoisophthalate, random copolymers of ethylene glycol and 1, 2-propane diol, the end groups consisting predominantly of sulfonated benzoate esters, followed by monoesters of ethylene glycol and/or propane diol. The aim is to obtain a polymer terminated at both ends with sulphonated benzoic acid groups, in the context of the present invention, the majority of said copolymers will be mainly terminated with sulphonated benzoic acid groups. However, some copolymers will not be fully capped and therefore their end groups may consist of monoesters of ethylene glycol and/or 1, 2-propylene glycol, thus constituting such minor species.

The selected polyester of the present invention comprises about 46 weight percent dimethyl terephthalate, about 16 weight percent 1, 2-propanediol, about 10 weight percent ethylene glycol, about 13 weight percent dimethyl ortho-sulfobenzoate and about 15 weight percent sulfonated isophthalic acid and has a molecular weight of about 3000. The polyester and the preparation method thereof are described in detail in EPA 311342.

It is well known in the art that free chlorine in tap water rapidly inactivates enzymes contained in detergent compositions. Thus, the use of chlorine scavengers such as perborate, ammonium sulphate, sodium sulphite or polyethyleneimine in the formulation in amounts above 0.1% by weight of the total composition will improve the wash stability of the detergent enzyme. Compositions containing chlorine scavengers are described in European patent application 92870018.6 filed on 31.1.1992.

Alkoxylated polycarboxylates, such as those prepared from polyacrylates, may be used herein to provide additional grease removal properties. Such materials are described in WO91/08281 and PCT90/01815, page 4, which is incorporated herein by reference. Chemically, these materials include polyacrylates having an ethoxy side chain for every 7-8 acrylate units. The side chain has the chemical formula: - (CH)₂CH₂O)_m(CH₂)_nCH₃M is 2 to 3 and n is 6 to 12. The side chains are ester-linked to the polyacrylate backbone to provide a "comb" polymer structure. The molecular weight may vary, but is generally in the range of from about 2000 to about 50,000. Such alkoxylated polycarboxylic acids may be included in the compositions of the present invention in an amount of from about 0.05% to about 10% by weight.

Dispersing agent

The detergent composition of the present invention may also comprise a dispersant: suitable water-soluble organic salts are the homopolyacids or the copolyoacids or their salts, in which the polycarboxylate contains at least two carboxyl groups separated from one another by not more than two carbon atoms. Polymers of this type are disclosed in GB-A-1,596,756. Examples of such salts are polyacrylates of molecular weight Mw2000-5000 and copolymers thereof with maleic anhydride, the molecular weight of such copolymers being 1,000-100,000.

In particular, copolymers of acrylates and methacrylates, such as 480N having a molecular weight of 4000, may be incorporated in the detergent compositions of the present invention at levels of from 0.5 to 20% by weight of the composition.

The composition of the present invention may comprise a lime soap peptizer compound, the Lime Soap Dispersability (LSDP), as defined below, preferably at most 8, preferably not more than 7, most preferably at most 6. The lime soap peptizer compound is preferably present in an amount of 0% to 20% by weight.

Numerical measurement of the effectiveness of lime soap peptizers is characterized by lime soap dispersant capacity (LSDP), which is determined using the lime soap dispersant test described in one of h.c. borghetty and c.a. bergman, j.am.oil.chem.soc., volume 27, pages 88-90, (1950). This calcium soap dispersion test method is widely used by professionals in the technical field to which the following review articles relate; linfield, Surfactant Science Series, Vol.7, p.3; n. linfield, Tenside surf.det., volume 27, pages 159-163, (1990); and m.k.nagarajan, w.f.masser, Cosmetics and Toiletries, volume 104, pages 71-73 (1989). LSDP is the weight percent ratio of dispersant to sodium oleate required to disperse lime soap deposits by dispersing 0.025g of sodium oleate in 30ml of CaCo having an equivalent hardness of 333ppm₃Formed in aqueous solution (Ca: Mg ═ 3: 2).

Surfactants having superior lime soap peptizer efficacy will include certain amine oxides, betaines, sultaines, alkyl ethoxy sulfates and ethoxylated alcohols.

Examples of the surfactant having an LSDP of at most 8 for use in the present invention include C₁₆-C₁₈Dimethylamine oxide, ethoxysulfuric acid C having an average degree of ethoxylation of from 1 to 5₁₂-C₁₈Alkyl esters with an average degree of ethoxylation of 3(LSDP ═ 4) ethoxysulfuric acid C₁₂-C₁₅Alkyl ester surfactants, in particular ethoxysulfuric acid C having an average degree of ethoxylation of 12(LSDP ═ 6) or 30₁₂-C₁₅Alkyl ester surfactants sold by BASF GmbH under the trade names Lutensol a012 and Lutensol a030, respectively.

Polymeric lime soap peptizers suitable for use in the present invention are described in an article by M.K. Nagarajan, W.F. Masler, Cosmetics and Toiletries, Vol.104, pp.71-73, (1989).

Hydrophobic bleaching agents such as 4- [ N-octanoyl-6-aminocaproyl ] benzenesulfonate, 4- [ N-nonanoyl-6-aminocaproyl ] benzenesulfonate, 4- [ N-decanoyl-6-aminocaproyl ] benzenesulfonate and mixtures thereof; and nonanoyloxybenzene sulphonate together with a hydrophilic/hydrophobic bleaching agent may also be used as the lime soap peptiser compound.

Dye transfer inhibition

The detergent compositions of the present invention may also comprise compounds for inhibiting the transfer of dissolved and suspended dyes from one fabric dye to another fabric encountered in fabric laundering operations involving colored fabrics.

Polymeric dye transfer inhibitors

The detergent compositions of the present invention also comprise from 0.001% to 10%, preferably from 0.01% to 2%, more preferably from 0.05% to 1% by weight of a polymeric dye transfer inhibiting agent. The polymeric dye transfer inhibiting agents are typically incorporated into detergent compositions for the purpose of inhibiting the transfer of dye from colored fabrics to fabrics laundered therewith. These polymers are capable of sequestering or adsorbing fugitive dyes that elute from colored fabrics before the dyes have an opportunity to adhere to other articles in the wash.

Particularly suitable polymeric dye transfer inhibiting agents are polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinylpyrrolidone polymers, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof.

The addition of such polymers may also enhance the performance of the enzymes of the invention.

a) Polyamine N-oxide polymers

Polyamine N-oxide polymers suitable for use comprise units having the following structural formula:

wherein:

p is a polymerizable unit to which R-N-O may be attached or wherein the R-N-O group may form part of the polymerizable unit, or a combination of both.

A is

-O-, -S-, -N-; x is 0 or 1;

r is an aliphatic, ethoxylated aliphatic, aromatic, heterocyclic or alicyclic group or any combination thereof to which the nitrogen of the N-O group may be attached or which may be part of the N-O group.

The N-O group can be represented by the following general formula:

wherein R is₁、R₂And R₃Is aliphatic, aromatic, heterocyclic or alicyclic group or combinations thereof, x or/and y or/and z is 0 or 1, and wherein the nitrogen of the N-O group may be attached thereto or the nitrogen of the N-O group may form part of these groups.

The N-O group may be part of the polymerizable unit (P) or may be attached to the polymer backbone, or a combination of both.

Suitable polyamine N-oxides in which the N-O group forms part of the polymerizable unit include polyamine N-oxides in which R is selected from aliphatic, aromatic, alicyclic or heterocyclic groups.

One such polyamine N-oxide includes polyamine N-oxides wherein the nitrogen of the N-O group forms part of the R group. Preferred polyamine N-oxides are those wherein R is a heterocyclic group such as pyridine, pyrrole, imidazole, pyrrolidine, piperidine, quinoline, acridine and derivatives thereof.

Another such polyamine N-oxide includes polyamine N-oxides wherein the nitrogen of the N-O group is attached to the R group.

Other suitable polyamine N-oxides are polyamine N-oxides wherein the N-O group is attached to a polymerizable unit.

Preferred such polyamine N-oxides are those having the general formula (I) wherein R is an aromatic, heterocyclic or alicyclic group to which the nitrogen of the N-O functionality belongs.

Examples of these types are polyamine oxides wherein R is a heterocyclic compound such as pyridine, pyrrole, imidazole and derivatives thereof.

Another preferred class of polyamine N-oxides are the polyamine N-oxides having the general formula (I) wherein R is an aromatic, heterocyclic or alicyclic group to which the nitrogen of the N-O functionality is attached.

Examples of these types are polyamine oxides in which the R groups can be aromatic groups, such as phenyl.

Any polymer backbone can be used as long as the amine oxide polymer formed is water soluble and has dye transfer inhibiting properties. Examples of suitable polymer backbones are polyethylene, polyolefins, polyesters, polyethers, polyamides, polyimides, polyacrylates and mixtures thereof.

The amine N-oxide polymer of the invention generally has a ratio of amine to amine N-oxide of from 10: 1 to 1: 1000000. However, the amount of amine oxide groups present in the polyamine oxide polymer can be varied by appropriate copolymerization or by appropriate degree of N-oxidation. Preferably, the ratio of amine to amine N-oxide is from 2: 3 to 1: 1000000, more preferably from 1: 4 to 1: 1000000, most preferably from 1: 7 to 1: 1000000. The polymers of the present invention comprise in fact random or block copolymers wherein one monomer type is an amine N-oxide and the other monomer type is either an amine N-oxide or not. The amine oxide units of the polyamine N-oxide have a pKa < 10, preferably a pKa < 7, more preferably a pKa < 6.

Polyamine oxides can be obtained at almost any degree of polymerization. The degree of polymerization is not critical, provided that the material has the desired water solubility and dye suspending ability.

Typically, the average molecular weight is within the range of 500-; preferably 1,000-50,000, more preferably 2,000-30,000, and most preferably 3,000-20,000.

b) Copolymers of N-vinylpyrrolidone and N-vinylimidazole

The average molecular weight of the N-vinylimidazole N-vinylpyrrolidone polymer used in the present invention is 5,000-1,000,000, preferably 5,000-200,000.

Highly preferred polymers for use in the detergent compositions of the present invention include polymers selected from the group consisting of N-vinylimidazole N-vinylpyrrolidone copolymers wherein the average molecular weight of the polymer is 5,000-50,000, more preferably 8,000-30,000, most preferably 10,000-20,000.

The average molecular weight ranges are determined by light scattering, as described in "modern methods of Polymer Characterization" published in Barth H.G. and Mays J.W. on Chemical Analysis, vol 113.

Highly preferred N-vinylimidazole N-vinylpyrrolidone copolymers have an average molecular weight of 5,000-50,000; more preferably 8,000-30,000; most preferably 10,000 and 20,000.

N-vinylimidazole N-vinylpyrrolidone copolymers having the stated average molecular weight range provide excellent dye transfer inhibition properties while not adversely affecting the cleaning performance of detergent compositions formulated therewith.

The molar ratio of N-vinylimidazole to N-vinylpyrrolidone in the N-vinylimidazole N-vinylpyrrolidone copolymers of the present invention is from 1 to 0.2, more preferably from 0.8 to 0.3, most preferably from 0.6 to 0.4.

c) Polyvinylpyrrolidone

The detergent compositions of the present invention may also employ polyvinylpyrrolidone ("PVP") having an average molecular weight of from about 2,500 to about 400,00, preferably from about 5,000 to about 200,000, more preferably from about 5,000 to about 50,000, most preferably from about 5,000 to about 15,000. Suitable polyvinylpyrrolidones are sold under the product names PVPK-15 (viscosity molecular weight 10,000), PVPK-30 (average molecular weight 40,000), PVPK-60 (average molecular weight 160,000), and PVPK-90 (average molecular weight 360,000) by ISP Corporation, New York, NY and Montreal, Canada. Other suitable polyvinylpyrrolidones commercially available from BASF corporation include Sokalan HP165 and Sokalan HP 12; polyvinylpyrrolidone is known to the person skilled in the art of detergents (see for example EP-A-262,897 and EP-A256,696).

d) Polyvinyl oxazolinone:

polyvinyl oxazolinones may also be used as polymeric dye transfer inhibitors in the detergent compositions of the present invention. The polyvinyl oxazolinone has an average molecular weight of about 2,500 to about 400,000, preferably about 5,000 to about 200,000, more preferably about 5,000 to about 50,000, most preferably about 5,000 to about 15,000.

e) Polyvinyl imidazole:

polyvinyl imidazoles may also be used as polymeric dye transfer inhibiting agents in the detergent compositions of the present invention. The polyvinylimidazole has an average molecular weight of from about 2,500 to about 400,000, preferably from about 5,000 to about 200,000, more preferably from about 5,000 to about 50,000, and most preferably from about 5,000 to about 15,000.

f) Crosslinked polymer:

crosslinked polymers are polymers whose backbones are linked to one another to some extent; these linkages, which may be chemical or physical, may be attached to reactive groups on the backbone or branches; crosslinked polymers have been described in Journal of Polymer Science, Vol.22, pp.1035-1039.

In one embodiment, the crosslinked polymer is prepared in a manner such that it forms a three-dimensional rigid structure that entraps the dye within the pores formed by the three-dimensional structure. In another embodiment, the crosslinked polymer entraps the dye by swelling. Such crosslinked polymers are described in co-pending patent application 94870213.9.

Washing method

The compositions of the present invention can be used in essentially any washing or cleaning process, including soaking, pretreatment and rinse-containing processes, and a process in which a separate rinse aid composition is added.

The method described in this invention involves contacting the fabric, dishware or any other hard surface with a wash liquor in a conventional manner, as will be exemplified below. Conventional laundry methods involve treating stained fabrics with an aqueous liquor containing an effective amount of a laundry detergent and/or fabric care composition dissolved or dispersed therein. Preferred machine dishwashing methods comprise treating soiled articles with an aqueous liquor containing an effective amount of a machine dishwashing or rinsing composition dissolved or dispersed therein. A conventional effective amount of a dishwashing machine composition means 8-60 grams of product dissolved or dispersed in a wash volume of 3-10 liters. According to the hand dishwashing method, soiled dishes are contacted with an effective amount, usually 0.5-20g (per 25 dishes to be treated) of the dishwashing composition. Preferred hand dishwashing methods include applying a concentrated solution to the surface of the dishes or dipping the dishes in a bulk dilute solution of the detergent composition. Conventional hard surface methods include treating soiled hard objects with, for example, sponges, brushes, cloths, and the like, which contain an aqueous liquid and/or undiluted such compositions that dissolve or dispense an effective amount of a hard surface cleaner. It also comprises impregnation into a concentrated or bulk dilute solution of the detergent composition. The method of the present invention can be conveniently carried out during the cleaning process. The washing process is preferably carried out at from 5 ℃ to 95 ℃, in particular from 10 ℃ to 60 ℃, and the pH of the treatment solution is preferably from 7 to 12.

The following examples are intended only to illustrate the compositions of the present invention and are not to be considered as limiting or otherwise defining the scope of the invention.

In detergent compositions, the enzyme amount is expressed as the amount of pure enzyme based on the total weight of the composition, and unless otherwise specified, the detergent ingredients are expressed as weights based on the total weight of the composition. Wherein the abbreviated component designations have the following meanings:

and (3) LAS: straight chain C_11-13Sodium alkyl benzene sulfonate.

TAS: sodium tallow alkyl sulphate

CxyAS：C_1x-C_1yAlkyl sodium sulfate

CxySAS：C_1x-C_1ySodium secondary (2, 3) alkylsulfate

CxyEz: c condensed with an average of z moles of ethylene oxide_1x-C_1yPredominantly linear primary alcohols

CxyEzS: c condensed with z moles of ethylene oxide_1x-C_1yAlkyl sodium sulfate

CxEOy: cy alcohol having an average degree of ethoxylation of y.

N11: an ethoxylated/propoxylated fatty alcohol, such as plurafac lf404, is mixed that is an alcohol having an average degree of ethoxylation of 3.8 and an average degree of propoxylation of 4.5.

N1 2：C₁₂-C₁₄Alkyl dimethyl amine oxide

QAS：R₂.N⁺(CH₃)₂(C₂H₄OH) wherein R₂＝C₁₂-C₁₄

QAS1：R₂.N⁺(CH₃)₂(C₂H₄OH) wherein R₂＝C₈-C₁₁

SADS：C_14-22Sodium alkyl sulfate of the formulaIs 2- (R) C₄H₇-1，4-(SO₄-)2, wherein R ═ C_10-18。

MBAS：C_12-18Medium branched alkyl sulfate surfactant with average degree of branching of 1.5 methyl or ethyl branched groups

MES：C₁₈X-sulfomethyl esters of fatty acids

APA：C₈-C₁₀Amidopropyldimethylamine

Soap: sodium linear alkylcarboxylates derived from 80/20 mixtures of tallow and coconut fatty acids

STS: sodium toluenesulfonate salt

TFAA：C₁₆-C₁₈Alkyl N-methylglucamides

TPKFA：C₁₂-C₁₄Fatty acid topped whole fraction

DEQA: bis (tallowoyloxyethyl) dimethylammonium chloride

DEQA (2): bis (soft-tallowyloxyethyl) hydroxyethyl ammonium methyl sulfate.

SDASA: stearyl dimethylamine in a 1: 2 ratio: triple extruded stearic acid.

DTMAMS: ditalloyl dimethyl ammonium methyl sulfate.

Silicate salt: amorphous sodium Silicate (SiO)₂∶Na₂O ratio is 1.6-3.2: 1).

Metasilicate: sodium metasilicate (SiO)₂∶Na₂O ratio 1.0).

Zeolite a: has a chemical formula of Na₁₂(AlO₂SiO₂)₁₂.27H₂O sodium aluminosilicate hydrate having a primary particle size of 0.1 to 10 μm (weight expressed as anhydrous base)

SKS-6: has a chemical formula of delta Na₂Si₂O₅Crystals of (2)Layered silicate

Citrate salt: citric acid trisodium dihydrate

Citric acid: anhydrous citric acid

Carbonate salt: anhydrous sodium carbonate

Bicarbonate salt: sodium bicarbonate

Sulfate: anhydrous sodium sulfate

Magnesium sulfate: anhydrous magnesium sulfate

STPP: anhydrous sodium tripolyphosphate

TSPP: tetrasodium pyrophosphate

MA/AA: 4: 1 acrylic acid/maleic acid random copolymer having an average molecular weight of about 70,000-80,000

MA/AA (1): 6: 4 acrylic acid/maleic acid random copolymer having an average molecular weight of about 10,000

AA: sodium polyacrylate polymer having an average molecular weight of 4,500

Polycarboxylate salt: copolymers containing carboxylated monomers, such as mixtures of acrylic, maleic and methacrylic acids, with molecular weights between 2,000 and 80,000, such as Sokolan, commercially available from BASF, which is an acrylic copolymer, with a MW of 4500.

Clay: bentonite or smectite.

PB 1: anhydrous sodium perborate monohydrate.

PB 4: general formula is NaBO₃.4H₂Sodium perborate tetrahydrate of O.

Percarbonate salts: general formula is Na₂CO₃.3H₂O₂Anhydrous sodium percarbonate of

NaDCC: sodium dichloroisocyanurate

TAED: tetra acetyl ethylene diamine

NOBS: nonoyloxybenzene sulfonic acid sodium salt

NACA-OBS: (6-nonanamide hexanoyl) oxybenzene sulfonate.

LOBS: sodium dodecyloxybenzenesulfonate

DOBA: dodecanoylbenzoic acid

DTPA: diethylene triamine pentaacetic acid

HEDP: 1, 1-hydroxyethane diphosphate

DETPMP: diethyltriaminepenta (methylene) phosphonate sold by Monsanto under the trade name Dequest 2060

EDDS: Ethylenediamine-N, N' -disuccinic acid sodium salt, (S, S) isomer

MnTACN: 1,4, 7-trimethyl-1, 4, 7-triazacyclononane manganese

Photosensitized bleaching agent: dextrin-soluble polymer encapsulated sulfonated zinc or aluminum phthalocyanine cyanines

PAAC: pentamine cobalt (III) acetate salt

Paraffin wax: paraffinic oil sold under the trade name Winog 70 by Wintershall

NaBz: sodium benzoate

Protease: proteolytic enzymes sold under the trade name Savinase by Novo Nordisk A/S, "protease B" variants with the substitution Y217L described in EP251446, "protease D" variants with the substitution combination N76D/S103A/V1041 and proteases with the substitution combination 101G/103A/1041/159D/232V/236H/245R/248D/252K amino acids described in WO99/20727, WO99/20726 and WO 99/20723.

Amylase: from Novo Nordisk A/S under the trade name Termamyl^And Duramyl^Amylases are sold, and those variants described in WO95/35382 with improved thermostability, having deletions of R181' + G182 or T183 + G184 amino acids

Lipase: lipolytic enzymes sold under the trade names Lipase, Lipolase Ultra by Novo Nordisk A/S and Lipomax by Gist Brocades

CGT-enzyme: cyclodextrin transferase sold under the name Tortuzyme by NovoNordisk A/S

AMG: amyloglucosidase sold under the name AMG by Novo Nordisk A/S

Cellulase: cellulases sold by Novo Nordisk A/S under the trade names Carezyme, Celluzyme and/or Endolase

CMC: sodium carboxymethyl cellulose

PVP: polyethylene polymer having an average molecular weight of 60,000

PVNO: polyvinylpyridine N-oxide with an average molecular weight of 50,000

PVPVI: copolymer of vinylimidazole and vinylpyrrolidone having an average molecular weight of 20,000

Whitening agent 1: disodium 4, 4' -bis (2-sulfostyrene) biphenyl

Whitening agent 2: 4, 4' -bis (4-anilino-6-morpholino-1, 3, 5-triazin-2-yl) stilbene-2: 2' -Disulfonic acid disodium salt

Whitening agent 3: 4, 4' -bis (4, 6-dianilino-1, 3, 5-triazin-2-yl) aminostilbene-2: 2' -Disulfonic acid disodium salt

Siloxane defoamer: a polydimethylsiloxane foam control agent, wherein a siloxane oxyalkylene copolymer is used as a dispersant, and the ratio of the foam control agent to the dispersant is 10: 1 to 100: 1.

And (3) foam inhibitor: 12% siloxane/silica, 18% stearyl alcohol, 70% granular starch

Thickening agent: high molecular weight crosslinked polyacrylates such as Carbopol supplied by b.f. goodrich chemical Company and Polygel.

SRP 1: anionic end-capped polyesters

SRP 2: a soil release polymer selected from the group consisting of 1) a non-cotton soil release polymer according to U.S. Pat. No. 5,415,807 issued 5/16/1995 to Pan, Kellett and Hall and/or 2) a non-cotton soil release polymer according to U.S. application 60/051517

QEA: bis ((C)₂H₅O)(C₂H₄O)_n)(CH₃)-N⁺-C₆H₁₂-N⁺-(CH₃) Bis (C)₂H₅O)-(C₂H₄O))_nWherein n is 20-30

PEI: polyethyleneimine having an average molecular weight of 600-1800 and an average degree of ethoxylation of 7-20 ethyleneoxy residues per nitrogen

SCS: sodium cumene sulfonate

HMWPEO: high molecular weight polyethylene oxide

PEGX: polyethylene glycol having a molecular weight of X

PEO: polyethylene oxide having an average molecular weight of 5,000

TEPAE: tetraethylenepentamine ethoxylate

A BTA: benzotriazole compounds

pH: measured as a 1% solution in distilled water at 20 deg.C

Example 1

A granular laundry detergent composition is prepared according to the invention as follows:

I II III IV V

spraying onto the dried granules

LAS 10.0 10.0 15.0 5.0 5.0

TAS - 1.0 - - -

MBAS - - - 5.0 5.0

C₄₅AS - - 1.0 - 2.0

C₄₅AE₃S - - - 1.0 -

QAS - - 1.0 1.0 -

DTPA, HEDP and/or EDDS 0.30.30.50.3-

Magnesium sulfate 0.50.50.1-

Citrate salt- - -3.05.0

Carbonate 10.07.015.0-

Sulfate 5.05.0- -5.0

Silicate- - -2.0

I II III IV V

Zeolite A16.018.020.020.0-

SKS-6 - - - 3.0 5.0

MA/AA or AA 1.02.011.0-

PEG 4000 - 2.0 0.1 - 3.0

QEA 1.0 - - - 1.0

Brightener 1 or 2 or 30.050.050.05-0.05

Silicon oil 0.010.010.01-

Agglomerates

Carbonate salt- - -4.0

SKS-6 6.0 - - - 6.0

LAS 4.0 5.0 - - 5.0

Granular component of dry additive

Maleic acid/carbonate/bicarbonate 8.010.010.04.0-

(40∶20∶40)

QEA - - - 0.2 0.5

NACA-OBS 2.0 - - 3.0 -

NOBS 1.0 3.0 3.0 - -

TAED 2.5 - - 1.5 2.5

MBAS - - - 8.0 -

LAS (sheet) 10.010.0-

Spray on

Brightener 1 or 2 or 30.20.20.30.10.2

Fragrance 1.00.51.10.80.3

Dry additives

Citrate- -20.04.0-

Percarbonate 15.03.06.010.0-

Perborate salt- - -6.0

Light activated bleach 0.020.020.020.10.05

Enzymes (cellulases, amylases, 0.040.010.020.020.05)

Protease and/or lipase)

CGT-enzyme 0.010.050.0020.0010.5

Carbonate 0.010.0-

Perfume (Encapsulated) -0.50.5-0.3

Suds suppressor 1.00.60.3-0.10

Soap 0.50.20.33.00.5

I II III IV V

Citric acid- -6.06.0

SKS-6 - - - 4.0 -

The filler is 100 percent

Example 2

I II III IV

blown powder

MES 2.0 0.5 1.0 -

SADS - - - 2.0

LAS 6.0 5.0 11.0 6.0

TAS 2.0 - - 2.0

Zeolite A24.0-20.0

STPP - 27.0 24.0 -

Sulfate 4.06.013.0-

MA/AA 1.0 4.0 6.0 2.0

Silicate 1.07.03.03.0

CMC 1.0 1.0 0.5 0.6

Whitening agent 10.20.20.20.2

Silicone suds suppressors 1.01.01.00.3

DTPMP 0.4 0.4 0.2 0.4

Spray on

Brightener 1 or 2 or 30.02-0.02

C45E7 - - 0.05 4.0

C45E2 2.5 - -

C45E3 2.5 - 0.05 -

Fragrance 0.50.30.50.2

Silicone suds suppressors 0.30.30.3-

Dry additives

QEA - - - 1.0

EDDS 0.3 - - -

Sulfate 2.03.05.010.0

Carbonate 6.013.015.014.0

Citric acid 2.5-2.0

I II III IV

QAS 0.5 - - 0.5

SKS-6 10.0 - - -

Percarbonate 4.03.0-1.9

NOBS 0.5 - - -

TAED 0.75 4.5 - -

Clay-10.0-

Protease 0.03-

Lipase 0.0080.0080.0080.004

CGT-enzyme 0.010.010.0010.004

Amylase 0.003-0.0030.006

Whitening agent 10.05-0.05

Other/auxiliary substances and microparticles added to 100%

Example 3

I II III IV V VI

blown powder

LAS 23.0 8.0 7.0 9.0 7.0 7.0

QAS - - - - 1.0 -

C45AS 6.0 6.0 5.0 8.0 - -

C45AE11S - 1.0 1.0 1.0 - -

MES 2.0 - - - 2.0 4.0

Zeolite A10.018.014.012.010.010.0

MA/AA - 0.5 - - - 2.0

MA/AA1 7.0 - - - - -

AA - 3.0 3.0 2.0 3.0 3.0

Sulfate 5.06.311.111.011.018.1

Silicate 10.01.01.01.01.01.0

Carbonate 15.020.010.020.78.06.0

PEG 4000 0.4 1.5 1.5 1.0 1.0 1.0

DTPA - 0.9 0.5 - - 0.5

Whitening agent 20.30.20.3-0.10.3

Spray on

C45E7 - - 0.5 - - 2.0

I II III IV V VI

C25E9 0.5 - - - - -

C23E9 - - 20 - 2.0

Fragrance 0.30.30.32.00.30.3

Agglomerates

C45AS - 5.0 5.0 2.0 - 5.0

LAS - 2.0 2.0 - - 2.0

Zeolite A-7.57.58.0-7.5

Carbonate-4.04.05.0-4.0

PEG 4000 - - 0.5 - - 0.5

Others (Water et al) -2.02.02.0-2.0

Dry additives

QAS I - - - - 1.0 -

Citric acid-2.0-

PB4 - - - - 5 -

PB1 - - 4 1.0 - -

Percarbonate 2.0-1.0-

Carbonate-5.31.8-4.04.0

NOBS 0.5 - 1.4 0.1 - -

Clay- -10.0

TAED 0.6 - 0.6 0.3 0.5 -

Methyl cellulose 0.2- - -0.5

DTPA 0.7 0.5 1.0 0.5 0.5 1.2

Microparticle- -0.20.5-

SKS-6 8.0 - - - - -

STS - - 2.0 - 1.0 -

1.0 to 2.0 parts of cumenesulfonic acid

Lipase 0.004-0.004-0.0040.008

Cellulase 0.00050.00050.00050.00070.00050.0005

Amylase 0.003-0.001-0.003-

CGT-enzyme 0.010.10.0050.0020.0010.05

AMG - - 0.001 0.001 - -

Protease 0.010.0150.0150.009-

PVPVI - - - - 0.5 0.1

PVP - - - - 0.5 -

I II III IV V VI

PVNO - - 0.5 0.3 - -

QEA - - - - 1.0 -

SRP1 0.2 0.5 0.3 - 0.2 -

Silicone suds suppressors 0.20.40.20.40.1-

Magnesium sulfate-0.2-

Adding other auxiliary materials to 100%

Example 4

I II III IV

elementary particles

STPP - 22.0 - 15.0

Zeolite A30.0-24.05.0

Sulfate 5.55.07.07.0

MA/AA 3.0 - - -

AA - 1.6 2.0 -

MA/AA 1 - 12.0 - 6.0

LAS 14.0 10.0 9.0 20.0

C45AS 8.0 7.0 9.0 7.0

C45AE11S - 1.0 - 1.0

MES 0.5 4.0 6.0 -

SADS 2.5 - - 1.0

Silicate-1.00.510.0

Soap-2.0-

Whitening agent 10.20.20.20.2

Carbonate 6.09.08.010.0

PEG 4000 - 1.0 1.5 -

DTPA - 0.4 - -

Spray on

C25E9 - - - 0.5

C45E7 10 1.0 - -

C23E9 - 1.0 2.5 -

Spice 0.20.30.3-

Dry additives

I II III IV

Carbonate 5.010.013.08.0

PVPVI/PVNO 0.5 - 0.3 -

Protease 0.030.030.030.015

Lipase 0.008-0.008

CGT-enzyme 0.0010.50.010.005

Amylase 0.002-0.002

Cellulase 0.00020.00050.00050.0003

DTPA 0.5 0.3 0.5 1.0

LOBS - 0.8 - 0.3

PB1 5 3.0 10 4.0

DOBA 1.0 - 0.4 -

TAED 0.5 0.3 0.5 0.6

Sulfate 4.05.0-5.0

SRP1 - 0.4 - -

Antifoam-0.5-

Microparticle 09-2.71.2

Adding other auxiliary materials to 100%

Example 5

I II III IV V VI VII

C13LAS 3 16.0 23.0 19.0 18.0 20.0 16.0

C45AS 4.5 - - - 4.0

C45AE(3)S - - 2.0 - 1.0 1.0 1.0

C45AE(3.0) 10.0 4.0 - 1.3 - - 0.6

C₉-C₁₄alkyldimethylhydroxy-1.00.52.0

Ethyl quaternary ammonium salt

Tallow fatty acid- - -1.0

STPP 23.0 25.0 24.0 22,0 20.0 15.0 20.0

Carbonate 15.012.015.010.013.011.010.0

AA 0.5 0.5 0.5 0.5 - - -

MA/AA - - 1.0 1.0 1.0 2.0 0.5

Silicate 3.06.09.08.09.06.08.0

I II III IV V VI VII

Sulfate 25.018.020.018.020.022.013.0

Sodium perborate 5.05.010.08.03.01.02.0

PEG 4000 1.5 1.5 1.0 1.0 - - 0.5

CMC 1.0 1.0 1.0 - 0.5 0.5 0.5

Citric acid 0.51.00.50.51.00.70.3

NOBS/DOBS 1.5 1.0 2.5 2.5 0.3 0.2 0.5

TAED 1.5 1.5 1.0 1.0 1.0 1.0 1.0

SRP2 7.5 7.5 6.0 7.0 5.0 3.0 5.0

Moisture content- -1.00.51.5

Mg

DTPA, HEDP and/or EDDS- - -0.80.61.0

CGT-enzyme 0.010.01.005.0050.10.1.0.001

Enzymes (Amylase, cellulase- - -0.050.040.05

And/or protease)

Small amounts of substances, such as perfumes, brighteners,

adding to 100 percent

Photobleaches, microgranules

Example 6

I II III IV

C13LAS 13.3 13.7 10.4 8.0

C45AS 3.9 4.0 4.5 -

C45AE(0.5)S 2.0 2.0 - -

C45AE(6.5) 0.5 0.5 0.5 5.0

C₉-C₁₄alkyl dimethyl hydroxy 1.0-0.5

Ethyl quaternary ammonium salt

0.5-property of tallow fatty acid

Tallow alcohol ethoxylate (50) - -1.00.3

STPP - 41.0 - 20.0

Zeolite A26.3-21.31.0

Carbonate 23.912.425.217.0

AA 3.4 0.0 2.7 -

MA/AA - - 1.0 1.5

Silicate 2.46.42.16.0

I II III IV

Sulfate 10.510.98.215.0

Sodium perborate 1.01.01.02.0

PEG 4000 1.7 0.4 1.0 -

CMC 1.0 - - 0.3

Citric acid-3.0-

NOBS/DOBS 0.2 0.5 0.5 0.1

TAED 0.6 0.5 0.4 0.3

SRP2 1.5 1.5 1.0 1.0

Water content 7.53.16.17.3

Magnesium sulfate- - -1.0

DTPA, HEDP and/or EDDS- - -0.5

Enzymes (amylases, cellulases, -0.025-0.04

Protease and/or lipase)

CGT-enzyme 0.020.050.0050.008

Other/auxiliary substances including perfume, added to 100%

Brighteners, photobleaches

Example 7

A tablet or granular laundry detergent composition is prepared according to the invention as follows:

I II III IV V VI

C13LAS 20.0 16.0 8.5 5 20.0 6.0

C45AS - 4.0 - - -

C45AE(3)S 1.0 1.0 - - - -

C45AE - 5.0 5.5 4.0 - 0.5

C₉-C₁₄alkyl dimethyl hydroxy 0.52.0 - - - -

Ethyl quaternary ammonium salt

1.0-taurine

STPP/Zeolite 10.020.030.020.025.025.0

Carbonate 41.030.030.025.045.024.0

AA - - - - - -

MA/AA 2.0 0.5 0.5 1.0 - -

Silicate 6.08.05.06.08.05.0

Sulfate 2.03.0- - -8.0

I II III IV V VI

Sodium perborate/sodium percarbonate 1.0-20.014.0-

PEG 4000 - 0.5 - - - 0.5

CMC 0.5 0.5 0.5 0.5 - 0.5

Citric acid- -

NOBS/DOBS 0.7 - - - - -

TAED/presynthesized peracid 0.7-2.53.5-

DTPA, HEDP and/or EDDS-0.50.5-

SRP 1.0 - 1.0 1.0 - -

Clay 4.03.07.010.06.08.0

PEO 1.0 0.5 2.0 0.5 1.0 0.5

Water content of 0.5-

0.5 to 0.5- -

Cellulose 2.0-1.5-1.0

Sodium acetate-1.00.54.01.0

Water content 3.05.05.05.08.010.0

Magnesium sulfate 0.51.5-

Soap/suds suppressors 0.61.01.00.80.5-

Enzymes (amylases, cellulases, 0.040.040.010.020.020.03)

Protease and/or lipase)

CGT-enzyme 0030.010.05.0030.01.005

Small amounts of substances, such as flavors, PVP,

PVPVI/PVNO, whitening agent, added to 100%

Photobleaches, microgranules

Example 8

Laundry detergent compositions were prepared according to the invention as follows:

I II III IV V

C13LAS 5.0 16.0 23.0 19.0 18.0

C45AS - 4.5 - - -

C45AE(3)S - - 2.0 - 1.0

C45AE 10 2.0 - 1.3 -

I II III IV V

C9-C14 alkyldimethylol- - -1.0

Ethyl quaternary ammonium salt

STPP/Zeolite 23.025.014.022,020.0

Carbonate 25.022.035.020.028.0

AA 0.5 0.5 0.5 0.5 -

MA/AA - - 1.0 1.0 1.0

Silicate 3.06.09.08.09.0

Sodium perborate/sodium percarbonate 5.05.010.0-3.0

PEG 4000 1.5 1.5 1.0 1.0 -

CMC 1.0 1.0 1.0 - 0.5

NOBS/DOBS - 1.0 - - 1.0

TAED/Per-acid 1.51.02.5-2.0

DTPA, HEDP and/or EDDS 0.50.50.5-1.0

SRP 1.5 1.5 1.0 1.0 -

Clay 5.06.012.07.010.0

Flocculant PEO 0.20.23.02.00.1

Wetting agent- -0.5

Paraffin 0.5- -

Cellulose 0.52.0-3.0

Sodium acetate 2.01.03.0-

Water content 7.57.56.07.05.0

Soap/suds suppressors-0.50.50.8

CGT-enzyme 0.0020.02.005.0050.01

Enzymes (amylases, cellulases, - -0.045)

Protease and/or lipase)

Other/auxiliary substances, e.g. perfumes

PVP, PVPVI/PVNO, added to 100%

Microparticles, brighteners, photobleaches

Example 9

Liquid laundry detergent compositions are prepared according to the present invention as follows:

I II III IV V VI

LAS - - - 1.0 2.0 -

C25AS 16.0 13.0 14.0 5.0 - 6.5

C25AE3S 5.0 1.0 - 10.0 19.0 3.0

C25E7 2.0 3.5 0.05 2.5 2.0 -

NI2 0.5 1.0 0.03 2.0 - -

TFAA 5.0 4.5 4.5 6.5 4.0 -

APA 2.0 1.0 - 3.0 - 0.5

QAS - - 2.0 - 1.5 -

TPKFA 4.5 8.0 15.0 - 5.0 5.0

citric acid 2.23.0-0.51.02.0

Fatty acid of rapeseed 2.0-3.06.01.5

Ethanol 3.22.02.52.2-0.5

1, 2-propanediol 5.78.56.57.07.05.5

Monoethanolamine 5.07.5-5.01.02.0

TEPAE - 1.2 - 0.5 0.5 -

PEI2 - 1.5 - 1.0 0.8 -

DTPMP 1.3 0.5 0.8 0.5 - 0.2

HEDP - 0.5 0.2 1.0 - -

Protease 0.02-0.020.020.020.01

CGT-enzyme 0.010.020.50.010.0050.002

AMG 0.001 0.001

Lipase 0.0020.0010.001-0.001-

Amylase 0008.0006.00060.0020.0010.001

Cellulase 0.0020.002-0.0020.001-

SRP1 0.20 0.15 0.10 - 0.17 0.04

PVNO - - - 0.05 0.10 -

Whitening agent 30.200.150.100.05-0.05

Suds suppressor 0.250.200.150.150.300.10

Calcium chloride 0.020.02-0.010.01-

Boric acid 2.52.01.52.21.51.2

Boron-moist soil-5.5-

NaOH to pH 8.07.57.78.07.07.5

Adding water/adjuvant to 100%

Example 10

A non-aqueous liquid laundry detergent composition is prepared according to the present invention as follows:

I II III

LAS 16.0 16.0 16.0

C23E05S 21.5 21.5 19.0

butoxy propoxy propanol 18.5-16.0

N12 0.05 1.0 2.0

Hexanediol-18.55.0

Sodium citrate dihydrate 6.86.83.8

[ NACA-OBS ] Na salt 6.06.06.0

Methyl tetrasubstituted polyethoxylated 1.31.31.3

Methylsulfate of hexamethylenediamine

EDDS 1.2 1.2 1.2

MA/AA - - 3.0

Sodium carbonate 10.010.010.0

Protease 0.05-0.02

CGT-enzyme 0.10.010.02

Amylase 0.010.010.01

Cellulase 0.00010.00010.0001

PB1 12.0 12.0 12.0

Silicone antifoam 0.750.751.1

Fragrance 1.71.71.7

0.50.50.5 dioxide

5, 12-dimethyl-1, 5,8, 12-0.030.03

Tetraazabicyclo [6.6.2]

Hexadecane manganese dichloride (II)

Whitening agent 20.20.20.2

Hydrogenated C16-18 fatty soap sodium 110.5

Colored particles 0.40.40.4

Adding others to 100%

Example 11

Laundry detergent compositions in tablet form were prepared according to the invention as follows:

i) a detergent base powder of composition 1 was prepared as follows: all of the particulate materials of the base composition 1 were mixed together in a mixing drum to form a homogeneous particulate mixture. During the mixing process, spraying was performed.

ii) the tablets are then prepared by: 50g of the matrix was introduced into a circular mold having a diameter of 5.5 cm and compacted to give a tensile strength (or radial breaking stress) of 10kPa to the tablet.

iii) the tablets were then dipped into a solution containing 90 parts by weight of sebacic acid and 10 parts by weight of Nymcel-ZSB16^TM(sold by Metsa Serla) in a bath at 140 ℃. RegulatingThe tablets were immersed in the hot bath for such a time that 4g of bath mixture was applied. The tablets were then left at ambient temperature of 25 ℃ for 24 hours. The tensile strength of the coated tablets increased to 30 kPa.

1

Anionic agglomerate 1 (40% anion, 27% zeolite and 33% carbonate) 21.5

Anionic agglomerate 2 (40% anion, 28% zeolite and 32% carbonate) 13.0

Cationic agglomerate (20% cation, 56% zeolite and 24% sulfate) 5.5

Layered silicate (95% SKS-6 and 5% silicate) 10.8

Sodium percarbonate 14.2

Bleach activator agglomerates (81% TAED, 17% acrylic acid-

Maleic acid copolymer (acid form) and 2% water 5.5

Carbonate salt 10.98

EDDS/sulphate granules (58% EDDS, 23% sulphate and 19% water) 0.5

HEDP 0.8

SRP 0.3

Fluorescent agent 0.2

Photosensitizing bleaching agent (zinc phthalocyanine sulfonate, 10% active) 0.02

Soap powder 1.4

Suds suppressor (11.5% silicone oil; 59% zeolite and 29.5% water) 1.9

Citric acid 7.1

CGT-enzyme 0.001

Protease 0.03

Lipase 0.006

Cellulase 0.0005

Amylase 0.02

PEG4000 1.0

Sprayed adhesive System (25% Lutensit K-IID 96; 75% by weight PEG) 4.0

Example 12

I II III IV V VI

first phase

Percarbonate-45.045.045.045.045.0

TAED - 9.7 9.7 9.7 9.7 9.7

Citric acid 10.015.020.015.015.015.0

STPP - - - - - 6.0

MA/AA 6.0 6.0 1.0 5.0 - -

Silicate salt- - -6.0-

Bicarbonate 15.015.010.015.015.015.0

N11 1.0 0.5 0.2 0.1 1.5 1.0

Carbonate 5.0- - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - -

Brightener 1 or 20.10.10.10.10.10.1

Fragrance 0.20.20.20.20.20.2

C12-16 fatty acid- - -1.0- - -

Protease 0.030.030.030.030.030.03

Amylase 0.020.02-0.02-

Second phase

CGT-enzyme 0.0010.0020.040.010.010.05

Protease 0.040.040.040.040.04-

Amylase 0.020.02-

Microparticles 0.090.090.090.090.090.09

PEG 4000 0.33 0.33 0.33 0.33 0.33 0.33

Citric acid 1.061.061.061.061.061.06

Bicarbonate 2.872.872.872.872.872.87

Example 13

Following preparation of laundry detergent bar compositions according to the invention (amounts given in parts by weight, enzymes expressed as pure enzymes):

I II III VI V III VI V

LAS - - 19.0 15.0 21.0 6.75 8.8 -

C28AS 30.0 13.5 - - - 15.75 11.2 22.5

sodium laurate 2.59.0-

Zeolite A2.01.25- - -1.251.251.25

Carbonate 20.03.013.08.010.015.015.010.0

Calcium carbonate 27.539.035.0-40.0

Sulfate 5.05.03.05.03.0- -5.0

TSPP 5.0 - - - - 5.0 2.5 -

STPP 5.0 15.0 10.0 - - 7.0 8.0 10.0

Bordeaux clay-10.0-5.0-

DETPMP - 0.7 0.6 - 0.6 0.7 0.7 0.7

CMC - 1.0 1.0 1.0 1.0 - - 1.0

Talc-10.015.010.0- -

Silicate- -4.05.03.0-

PVNO 0.02 0.03 - 0.01 - 0.02 - -

MA/AA 0.4 1.0 - - 0.2 0.4 0.5 0.4

SRP 1 0.3 0.3 0.3 0.3 0.3 0.3 0.3 0.3

Amylase-0.01- - -0.002-

CGT-enzyme 0.010.010.020.0020.050.010.010.002

Proteinase-0.004-0.0030.003-0.003

Lipase-0.002-0.002-

Cellulase- -. 0003- -. 0003.0002- - -

PEO - 0.2 - 0.2 0.3 - - 0.3

Spice 1.00.50.30.20.4-0.4

Magnesium sulfate-3.03.03.0-

NI2 5.0 - 2.0 - - 0.2 0.1 -

Whitening agent 0.150.10.15- - -0.1

Photosensitized-15.015.015.015.0-15.0

Bleaching agent (ppm)

Example 14

A granular fabric detergent composition capable of providing "softening" efficacy is prepared according to the invention as follows:

I II

C45AS - 10.0

LAS 7.6 -

C68AS 1.3 -

C45E7 4.0 -

C25E3 - 5.0

coconut oil based alkyl dimethyl hydroxyethyl ammonium chloride 1.41.0

Citrate 5.03.0

Na-SKS-6 - 11.0

Zeolite A15.015.0

MA/AA 4.0 4.0

DETPMP 0.4 0.4

PB1 15.0 -

Percarbonate-15.0

TAED 5.0 5.0

Smectite clay 10.010.0

HMWPEO - 0.1

Protease 0.020.01

Lipase 0.020.01

CGT-enzyme 0.050.02

Amylase 0.030.005

Cellulase 0.001-

Silicate 3.05.0

Carbonate 10.010.0

Suds suppressor 1.04.0

CMC 0.2 0.1

Adding other materials and adjuvants to 100%

Example 15

Rinse compositions incorporating fabric softener were prepared according to the invention as follows:

DEQA(2) 20.0

cellulase 0.001

CGT-enzyme 0.005

C45E01-3 1.0

HCL 0.03

Defoaming agent 0.01

Blue dye 25ppm

CaCl₂ 0.20

Perfume 0.90

Others and water are added to 100 percent

Example 16

Fabric conditioner compositions incorporating fabric softener and dryer were prepared according to the invention as follows:

I II III IV V

DEQA 2.6 19.0 - - -

DEQA(2) - - - - 52.0

DTMAMS - - - 26.0 -

SDASA - - 70.0 42.0 40.2

stearic acid 0.3- -

C45E01-3 1.0 0.5 13.0 0.5 0.2

HCL 0.02 0.02 - - -

Ethanol-1.0- -

Fragrance 0.31.00.751.01.5

Glycoperse S-20 - - - - 15.4

Glyceryl monostearate-26.0-

Geraniol succinate-0.38-

Polysiloxane antifoaming agent 0.010.01-

Electrolyte-0.1-

Amylase-0.2-0.20.2

CGT-enzyme 0.10.20.0010.010.01

Clay- - -3.0-

Dye 10ppm 25ppm 0.01-

100% of water and auxiliary substances 100-

Example 17

A compact, high density (0.96kg/l) dishwashing detergent composition was prepared according to the present invention as follows:

I II III IV V VI

STPP - 51.0 51.0 - - 44.3

citrate 17.0- -50.040.2-

Carbonate 17.514.020.0-8.033.6

Bicarbonate salt- - -26.0- - -

Silicate 15.015.08.0-25.03.6

Metasilicate 2.54.54.5-

PB1 10.0 8.0 8.0 - - -

PB4 - - - 10.0 - -

Percarbonate- -11.84.8

NI1 2.0 - 1.5 3.0 1.9 5.9

TAED 2.0 - - 4.0 - 1.4

HEDP 1.0 - - - - -

DETPMP 0.6 - - - - -

MnTACN - - - - 0.01 -

PAAC - 0.01 0.01 - - -

Paraffin 0.50.40.40.6-

Protease 0.070.050.050.03-0.01

Amylase 0.010.01-0.006

AMG 0.001 - - - - 0.01

CGT-enzyme 0.020.20.0021.00.0020.02

Lipase-0.001-0.005-

BTA 0.3 0.2 0.2 0.3 0.3 0.3

Polycarboxylate 6.0- - -4.00.9

Fragrance 0.20.10.10.20.20.2

pH 11.0 11.0 11.3 9.6 10.8 10.9

Others, sulfate and water added to 100%

Example 18

A granular dishwashing detergent composition having a bulk density of 1.02Kg/L was prepared according to the present invention as follows:

I II III IV V VI

STPP 30.0 33.5 27.9 29.6 33.8 22.0

carbonate 30.530.530.523.034.545.0

I II III IV V VI

Silicate 7.07.512.613.33.26.2

Metasilicate-4.5- -

Percarbonate- -4.0-

PB1 4.4 4.5 4.3 - - -

NADCC - - - 2.0 - 0.9

NI1 1.0 0.7 - 1.9 0.7 0.5

TAED - - 1.0 1.0 0.9 -

PAAC - 0.004 - - - -

Paraffin 0.250.25-

Protease 0.0360.0210.03-0.006-

Amylase 0.030.005-0.005-

CGT-enzyme 0.20.020.0022.00.020.005

0.005-0.001 of lipase

BTA 0.15 0.15 - - 0.2 -

Spice 0.20.20.050.10.2-

pH 10 8 11.3 11.0 10.7 11.5 10.9

Others, sulfate and water added to 100%

Example 19

Detergent compositions in tablet form were prepared according to the invention by using a standard 12-head rotary press at 13KN/cm²Compressing a granular dishwashing detergent composition under pressure of (a):

I II III IV V VI VII VIII

STPP - 48.8 54.7 38.2 - 52.4 56.1 36.0

citrate 20.0-35.9-

Carbonate 20.05.014.015.48.023.020.028.0

Silicate 15.014.815.012.623.42.94.34.2

Protease 0.0420.0720.0420.0310.0520.0230.0230.029

Amylase 0.0120.0120.0120.0070.0150.0030.0170.002

CGT-enzyme 0.020.010.0020.50.0080.0020.0020.02

0.005-Lipase

PB1 14.3 7.8 11.7 12.2 - - 6.7 8.5

PB4 - - - - 22.8 - 3.4 -

Percarbonate- -10.4- -

NI1 1.5 2.0 2.0 2.2 1.0 4.2 4.0 6.5

I II III IV V VI VII VIII

PAAC - - 0.02 0.009 - - - -

MnTACN - - - - 0.007 - - -

TAED 2.7 2.4 - - - 2.1 0.7 1.6

HEDP 1.0 - - 0.9 - 0.4 0.2 -

DETPMP 0.7 - - - - - - -

Paraffin 0.40.50.50.5-0.5-

BTA 0.2 0.3 0.3 0.3 0.3 0.3 0.3 -

Polycarboxylate 4.0- - -4.90.60.8-

PEG 4000-30000 - - - - - 2.0 - 2.0

Glycerol- - -0.4-0.5

Perfume- - -0.050.20.20.20.2

Tablet weight 20g 25g 20g 30g 18g 20g 25g 24g

pH 10.7 10.6 10.7 10.7 10.9 11.2 11.0 10.8

Others, sulfate and water added to 100%

Example 20

A liquid dishwashing detergent composition having a bulk density of 1.40Kg/L is prepared according to the present invention as follows:

I II III IV

STPP 17.5 17.2 23.2 23.1

carbonate-2.4-

Silicate 6.124.930.722.4

NaOCl 1.1 1.1 1.1 1.2

Thickener 1.01.11.11.0

NI1 0.1 0.1 0.06 0.1

NaBz 0.7 - - -

CGT-enzyme 0.0050.0020.0050.02

NaOH 1.9 - - -

KOH 3.6 3.0 - -

Spice 0.05- -

pH 11.7 10.9 10.8 11.0

Adding water to 100%

Example 21

The following dishwashing compositions in tablet form were prepared according to the invention (amounts given in grams):

I II III IV V VI

first phase

STPP 9.6 9.6 10.4 9.6 9.6 11.5

Silicate 0.50.71.61.01.02.4

SKS-6 1.5 1.50 2.30 2.25

Carbonate 2.32.73.53.64.15.2

HEDP 0.2 0.2 0.2 0.3 0.3 0.3

PB1 2.4 2.4 2.4 3.7 3.7 3.7

PAAC 0.002 0.002 0.002 0.003 0.004 0.004

CGT-enzyme 0.010.0020.050.0020.0011.0

Amylase 0.0020.0010.0010.0040.0030.003

Protease 0.002-0.0020.0030.0030.003

NI1 0.4 0.8 0.8 1.2 1.2 1.2

PEG 6000 0.4 0.3 0.3 - 0.4 -

BTA 0.04 0.04 0.04 - 0.06 0.06

Paraffin 0.10.10.10.150.150.15

Fragrance 0.020.020.020.010.010.01

Sulfate salt- - -0.50.052.3

Second phase

CGT-enzyme 0.0030.0030.0020.010.010.01

Amylase 0.00050.00050.00040.00050.0060.0004

Protease 0.0090.0080.010.0090.0080.01

Citric acid 0.30.30.30.30

Sulfamic acid-0.3-

Bicarbonate 1.10.40.41.10.40.4

Carbonate-0.5-

Silicate salt-0.6

CaCl₂ - 0.07 - - 0.07 -

PEG 3000 0.06 0.06 0.06 0.06 0.06 0.06

The multiphase sheet compositions were prepared as follows. Phase 1 detergent-active compositions are prepared by mixing the granules and liquid components and then feeding them into the mould of a conventional rotary press comprising a ram suitably shaped to form a mould. The cross section of the die is approximately 30 x 38 mm. The composition was then subjected to a pressure of 940kg/cm2, after which the punch was raised to expose the first photo agent comprising the mold on its upper surface. In the same manner, a phase 2 detergent active composition was prepared and fed into the die, and the granulated active composition was then subjected to a pressure of 170kg/cm2, the punch was raised, and the multi-phase tablet was ejected from the tablet press. The resulting tablet dissolved or disintegrated in the washing machine within 12 minutes as described above, and phase 2 of the tablet dissolved within 5 minutes. The tablets provide excellent dissolution and cleaning characteristics, and have excellent tablet integrity and strength.

Example 22

Hand dishwashing compositions were prepared according to the invention as follows:

I II III IV V VI VII VIII

C12-14E0-3S 26.0 34.2 25.0 26.0 37.0 26.0 22.0 32.0

C11LAS - - - - - - 13.0 -

c12-14 amine oxide 2.04.92.1-5.56.51-

C12-14 betaine 2.05.02.1- - -4.0

C12-14 glucamide 1.51.53.1- -

C9-11E8-9 4.5 1 4.1 3.0 1.0 3.0 - 1.0

Alkyl polyglucosides-12.03.0

C1-20 monoethanolamine- - -1.5-

DTPA - 0.1 0 0-500 0-500 0-500 0 0

ppm ppm ppm

Succinic acid-0-4.5

Cumene sulfonate-4.51 to 6-1 to 6- -

Calcium or sodium xylene sulfonate 5.0-4.0-2.5-

Magnesium salt (% Mg) 0.50.70.50.040.60.040.30

1, 3-bis (methylamino) cyclohexane- - -0.5-0.5- -

N, N-dimethylaminoethyl-0.2-0.2- -

Methacrylate homopolymers

I II III IV V VI VII VIII

Citric acid-0-3.50-3.5- -

Ethanol 6-85-86-94-107.04-104.04.0

Protease- - -0.08- -

CGT-enzyme 0.05.002.0050.010.40.050.0020.01

Amylase- -0.002-0.0050.040.05

Carbonate- -2.5- -

Polypropylene glycol (MW2000-4000) - - -0 to 2- -

pH 7-8 7-8 7-8 8.5-11 7-8 8.5-11 7 7

Perfume 0.1-0.7

The others (water and auxiliary substances) are added to 100 percent

Example 23

Fabric and hard surface cleaner compositions were prepared according to the invention as follows:

sulfate 18.5

Bicarbonate 18.6

Polycarboxylate 4.1

C₁₈Alpha-olefins 0.2

Enzyme (lipase, protease and/or cellulase) 0.004

Amylase 0-003

CGT-enzyme 0.05

Whitening agent 20.1

NI1 1.0

Photoactivated bleaching agent 0.04

Coated sodium percarbonate 45.0

TAED 8.8

Citric acid 2.5

Fragrance 0.1

Others and water are added to 100 percent

Claims

1. A detergent composition comprising a cyclodextrin glucanotransferase enzyme and a detergent ingredient selected from a nonionic surfactant, a protease, a bleaching agent and/or mixtures thereof.

2. A detergent composition according to claim 1 wherein said cyclodextrin glucanotransferase enzyme is comprised at a level of from 0.0002% to 10%, preferably from 0.001% to 2%, more preferably from 0.001% to 1% pure enzyme by weight of the total detergent composition.

3. A detergent composition according to claims 1-2 further comprising a starch binding domain.

4. A detergent composition according to claim 3 wherein said cyclodextrin glucanotransferase enzyme has or has incorporated a starch binding domain.

5. A detergent composition according to claims 1-4 wherein said nonionic surfactant is selected from polyethylene oxide condensates of alkyl alcohols, amide oxides, polyethylene oxide condensates of alkyl acids and/or mixtures thereof.

6. A detergent composition according to claims 1-5 wherein said bleach is selected from [ Mn (5, 12-dimethyl-1, 5,8, 12-tetraaza-bicyclo [6.6.2]]Hexadecane) Cl₂](ii) a [ Mn (5, 12-diethyl-1, 5,8, 12-tetraaza-bicyclo [6.6.2]]Hexadecane); a combination of percarbonate and a hydroxy benzene sulfonate selected from nonanoyloxybenzene sulfonate, N-nonanoyl-6-aminocaproic acid and/or tetraacetylethylenediamine; and/or mixtures thereof.

7. A detergent composition according to claims 1-6 wherein the protease is selected from the group consisting of protease Subtilisin 309 from Bacillus subtilis, "protease B" variant with Y217L substitution described in EP251446, "protease D" variant with N76D/S103A/V1041 substitution combination and proteases with 101G/103A/1041/159D/232V/236H/245R/248D/252K amino acid substitution combination described in WO99/20727, WO99/20726 and WO99/20723 and/or mixtures thereof.

8. A detergent composition according to claims 1-7 further comprising an enzyme selected from lipase, alpha-amylase, maltogenic alpha-amylase, amyloglucosidase and/or mixtures thereof.

9. Use of a cyclodextrin glucanotransferase enzyme and a detergent ingredient selected from a nonionic surfactant, a protease, a bleaching agent and/or mixtures thereof in a detergent composition for hydrolysing retrograded and/or raw starch.

10. Use according to claim 9 for the removal of starch-containing stains and soils and when formulated as laundry compositions, excellent whiteness maintenance and soil cleaning.